(Programme Project Report)

PPR

Bachelor of Science Honors (Biochemistry)

Directorate of Distance Education

NIMS UNIVERSITY RAJASTHAN, JAIPUR

Programme Project Report (PPR)

Bachelor of Science -Honors (Biochemistry)

A. Programme mission & Objectives:

Program Mission

To provide affordable higher education for the people from all walks of life and build

employability for each learner by degree meaningfully to career.

To achieve national and international recognition through education and research.

To emphasize the need and importance of innovation.

1 Degree Awarding body Nims University Rajasthan, Jaipur

2 Teaching Institution Directorate of Distance Education, Nims

University Rajasthan, Jaipur

3 Name of the Programme (Specified by UGC

etc.) Bachelor of Science (Hons.) (Biochemistry)

4 Minimum duration of the Programme (yrs.)

as per UGC norms Three Years

5 Minimum eligibility for admission 10+2 in any discipline in Science

6 Programme Credit 96

7 Qualifications framework level Graduate

8 Nature of Target Group of Learners Adults/ Professionals/In service Personnels/ Drop

outs / Home Makers

9 Date of Commencement Academic Year 2018-19

10 Type of Programme General

Program Objective

The program will provide highly developed skills in written communication, problem-solving,

critical thinking and interpersonal understanding.

Basic Knowledge will apply for identification, formulation, creation, construction, design,

development and optimization of various problems related to various fields of Chemistry and

Biology.

To prepared the leaner’s for successful pursuit of graduate studies and shall have abilities to engage

in lifelong learning in various field and to understand the challenges of a dynamically and

globalized changing world adapting their skills through continuous learning and self-improvement.

The program cultivates in Learners the values and attitudes to become a successful professional by

demonstrating logical and analytical thinking abilities.

B. Relevance of the program with HEI’s Mission and Goals:

Institutional Mission:

Nims University Rajasthan provides Outstanding Learning Experience for Excellence in all

discipline of Education and have a transformative impact on Society through continual innovation

in Education, Research and Entrepreneurship.

To prepare the students and scholars to take the challenges of present and future.

To promote the building up of character in youth as an integral part of education.

Institutional Goals

To provide affordable education to the society in all walks of life.

To provide advanced modern technical and other Professional courses with emphasis on developing

value based ethical career orientation.

To carry out cutting-edge research and development for the benefit of society

To produce skilled and competent manpower with commitment to societal needs.

To develop employability and entrepreneurship of stakeholders.

While designing and developing the curriculum, employability factor is given due consideration by

incorporating the industry requirements.

Linkage with Program Mission:

This program delivers required theoretical and industry inputs to students that develops creative

thinking to make them experts and professionals in the field.

The programs offered allow the learners to learn at their own pace along with pursuing their other

professional endeavors.

The students' support services are provided to enhance overall quality standards.

In all, the programs offered by Nims Directorate of Distance Education ensure continuous

education and meeting the needs of all class of learners.

C. Nature of prospective target group of learners:

The University envisions holistic development of the learners through distance education which is

very well reflected in the academic programmes.

The university adopts a systematic process for designing and developing the curriculum.

Curriculum is designed taking into consideration the guidelines / specifications prescribed by the

University Grants Commission.

The curriculum of Bachelor of Science (Hons.) Biochemistry is designed to help the students of

target groups primarily those who dropouts due to financial and social hurdles as well as due to any

personal reasons, low income groups (not able to afford cost of regular mode of education), rural

populations, labor class, employed persons etc.

It opens opportunity to the populations of any age group and sex, any professionals to acquire

higher education at low cost.

D. Appropriateness of programme to be conducted in open and distance learning mode to

acquire specific skills and competence:

Bachelor of Science (H) Biochemistry program covers all fields of biology, so that student excels in

multidisciplinary branches of science and research for lifelong engagements in the rapidly changing

field of science and related field.

Nims as a distance learning institution plays important role by providing flexible and cost effective

education to enhance productivity skills.

Provision of appropriate skills may thus be an important intervention to increasing the productivity

of employment workforce.

Distance education is more costs effective and can take place while continuing full-time

employment.

Program Learning Outcome

B.Sc. (Hons.) Biochemistry Program is geared to enable learners to:

Provide a systematic understanding of core science concepts, principles and theories along with

their applications.

Evaluate hypotheses, theories, methods and evidence within their proper contexts.

Solve complex problems by critical understanding, analysis and synthesis.

Communicate effectively by oral, written, computing and graphical means.

Imbibe domain-specific knowledge and develop globally-relevant skills for academic and

professional enhancement.

E. Instructional Design:

Course Curriculum:

The curriculum is designed and prepared by the committee of experts from the concerned departments and

the professionals of the Industries and experts from the different public and private sectors. The curriculum

is based on the industries and local, regional as well as national and International needs.

Program Structure:

B.Sc. (Honos.) Biochemistry Program is three year distance education program with 96 credits that are

divided in to 32 credit hours for each year.

Scheme: Bachelor of Science (Hons.) Biochemistry

YEAR- I

Course Title University

Examination

Internals

Assessment

Credits

Communication for Professionals 70 30 3

Cell Biology 70 30 4

Bioinformatics 70 30 4

Bio molecules 70 30 3

Plant Biochemistry 70 30 4

Enzymology 70 30 4

Cell Biology (P) 35 15 3

Bioinformatics (P) 35 15 3

Biomolecules (P) 35 15 4

750 32

YEAR II

Course Title

University

Examination

Internals

Assessment

Credits

Instrumentation and Techniques 70 30 4

Molecular Genetics 70 30 4

Immunology 70 30 4

Intermediary Metabolism 70 30 4

Membrane Biology 70 30 3

Molecular Genetics (P) 35 15 3

Immunology(P) 35 15 3

Intermediary Metabolism (P) 35 15 3

Seminar 100 4

750 32

YEAR III

Course Title University

Examination

Internals

Assessment

Credits

Environmental Science and Ecology 70 30 5

Industrial Biochemistry 70 30 5

Nutritional Biochemistry 70 30 4

Clinical Biochemistry 70 30 4

Industrial Biochemistry (P) 35 15 4

Clinical Biochemistry (P) 35 15 4

Project Work/ Industrial Training 200 6

700 32

Detail Syllabus is attached as annexure-I

Study Materials:

Distance learning is learning remotely, the quality of the study materials in the form of print

(Modules) and audio-visuals are provided by the Nims Directorate of Distance Education, which are

duly designed and developed by the team of experts.

The quality of study materials, combined with the tutor support and the range of other supports,

Nims Directorate of Distance Education is committed to best possible position to excel in studies.

Programs are offered on annual basis. The breakup of one credit worth of student effort, namely 32

hrs, typically has the following components. Academic activities are linked together to engage

learner and maximize learning.

Study Time Approx. Percentage of Credit

Print material including Audio/Video material 55%

Work related exercises practical/Quizzes and Assignments 25%

Through Web conferencing tool/internet based 20%

Duration of the Program: 3 Years

Faculty and support staff requirement:

01 (Assistant Professor)

Supporting staff will provided by directorate of distance education

Student Support Service Systems

Pre-Joining Support:

Information regarding Programs, Courses, Eligibility, Admission Procedures, Fee Structures,

Functions, Rules, and Regulations of the Institute, Recognitions, special features of the

programsetc are provided to the student.

Counseling services is also provided to individuals to the best way of achieving academic and

career goals.

On-Joining Support:

Study Material: Comprehensive printed study material, specially designed for self-study, shall be

provided to every learner. In addition to the study material, the learners are required to read

suggested text books, articles published in journals and follow the audio / video CDs, etc.

Video Lessons: To supplement the print material, NIMS prepares video lessons.

Library: Library facility is also available at central library and departmental/college library at

NIMS University Jaipur where course-wise textbooks shall be available for the use of learners.

The learners are provided with progress on assignments, examinations, Project work and

extension of program if student is not able to complete the program in stipulated period.

Personal Contact Program:

A 25 days Personal Contact Programme will be conducted to help the students to interact with

the faculty and get their queries and doubts resolved.

F. Procedure for Admissions, Curriculum Transaction and Evaluation

Procedure for Admissions

The University will notify Academic Calendar of Programs/Courses in newspaper and on

University website.

Admission to all the programmes is through notification in newspaper and on University website.

Admission process is online.

Eligibility Criteria for admission – 10+2 in any discipline in Science

Fee structure : Rs 12000/- Per Annum

Curriculum transactions :

Nims has established a robust Academic Delivery mechanism to ensure Quality Education at every stage.

Supply of Print Material

Periodic review of Curriculum and Study material

Systematic and structured Personal Contact Programs

User friendly LMS as Learning platform

Full-fledged archived class-room recorded lectures

Our Self–paced courseware has clear and measurable Learning outcomes; outcome is assessed with the

Continuous and Summative Assessment process. Course Delivery Plan is given to the students at the

commencement of new Academic Session.

The Academic Calendar includes all teaching-learning activities, for complete academic year.

Teaching Pedagogy

Our primary focus is on maximizing knowledge, developing competencies and inculcating of professional

ethics and values. Therefore, we employ andragogical (moving away from pedagogy) approaches and

principles that support self-directed and autonomous learning methodologies.

Evaluation

The evaluation system followed in institution includes both the Term End Examination (TEE) and Continuous

Evaluation.

Method of Evaluation for each Programme

Programme Continuous Evaluation

Weightage

in overall

assessment

Term and

Evaluation

Weightage

in overall

assessment

Bachelor Level

(Theory &

Practical)

Internal Assessment

(Assignments + Project Report) 30

Theory

Examination,

Practical & Viva

Voce

70

G. Requirement of the laboratory support and Library Resources:

Our Self Learning Material (SLM) serves the purpose of resource materials (print and digital content such as

videos, webinars, presentations, quizzes) designed to empower the leaner’s to achieve all their academic goals

and transform them to become an independent and autonomous reflective practitioners. In true sense, these

materials make them learning enjoyable, meaningful, transferrable, and permanent.

A major portion of our academic programmes are supported with Personal Contact Programs (PCP).

H. Cost Estimate of the Program and the Provisions:

S.NO. PERTICULARS AMOUNT PER ANNUM (Rs)

1. Course Fee 12,00,000/-

2. Self-Learning Materials development and distribution 10,00,000/-

3. Postal Expenses 10,00,000/-

4. Salary and other administrative 8,00,000/-

I. Quality assurance mechanism and expected program outcomes :

Nims University Rajasthan has constituted Internal Quality Assurance Cell (IQAC) which is responsible for the

monitoring of the quality of all programmes running under ODL programmes.

IQAC has a mandate to review the teaching and learning process. The Primary aim of the IQAC is to develop a

system for conscious, consistent and catalytic action to improve the academic and administrative performance

of the institution.

Expected program outcomes

Bachelor of Science (Hons.) Biochemistry Program is geared to enable learners to:

Provide a systematic understanding of core science concepts, principles and theories along with

their applications.

Evaluate hypotheses, theories, methods and evidence within their proper contexts.

Solve complex problems by critical understanding, analysis and synthesis.

Communicate effectively by oral, written, computing and graphical means.

Imbibe domain-specific knowledge and develop globally-relevant skills for academic and

professional enhancement.

The programme project report along with syllabus has been approved by the Board of Studies of the

Departments.

Annexure-I

Syllabus

Bachelor of Science (Hons.) (Biotechnology)

YEAR I

COMMUNICATION FOR PROFESSIONAL

Course Learning Objectives:

a. To impart knowledge of speech, verb and clauses.

b. To make students understand about report and paragraph making.

c. To impart knowledge of phrasal verbs and make them to communicate.

d. To make students learn about Indian literature.

e. To make students improve their vocabulary.

Course Detail:

UNIT

CONTENT

1

Essentials of Grammar: Parts of Speech; Vocabulary building; Sentence; Articles;

Pronouns; Quantity; Adjectives; Adverbs; Prepositions, Adverb particles and phrasal verbs,

Verb; Verb tenses; Imperatives; Active and passive voice; Direct and indirect speech; The

infinitive; Conditional sentences; Synonyms and antonyms; Singular and Plural; Figures of

Speech; Punctuation and Phonetics.

2

Nature, Scope and Process of Communication: Defining Communication; Nature of

Communication; Objectives/Purpose of Communication; Functions of Communication;

Process of Communication; Elements of Communication Process; Process of Communication:

Models; Working of the Process of Communication; Forms of Communication.

3

Channels and Networks of Communication: Channels of Communication; Communication

Flow in Organizations: Directions/Dimensions of Communication; Patterns of Flow of

Communication or Networks; Factors Influencing Organizational Communication.

4 Principles of Effective Communication: Communication Effectiveness: Criteria of

Evaluation; Seven Cs of Effective Communication; Four Ss of Communication.

5

Barriers in Communication: Categorization of Barriers; Semantic Barriers; Organizational

Barriers Interpersonal Barriers (Relating to Superior-subordinate); Individual or Psycho-

sociological Barriers; Cross-cultural/Geographic Barriers; Physical Barriers/Channel and

Media Barriers; Technical Aspects in Communication Barriers; Overcoming the Barriers in

Communication; Measures to Overcome Barriers in Communication.

6 Non-verbal Communication: Characteristics of Non-verbal Communication; Relationship of

Non-verbal Message with Verbal Message; Classification of Non-verbal Communication.

7

Oral Communication: Informal Conversation: Oral Communication; Informal

Conversation; Learning Informal Conversation; How to Go About Learning Other Tricks?;

Learning Conversational Skills; Internet Chat.

8

Communication in Business Organizations: Meaning of Business Communication; Types

of Information Exchanged in Business Organizations; Role of Communication in Business

Organizations; Importance of Communication in Management of Business Organizations;

Scope of Communication in Organizational Setting; Characteristics of Effective Business

Communication; New Communication Environment; Ethical challenges and Trapsin

Business Communication; Role of Communication in Three Managerial Roles Defined by

Henry Mintzberg.

9 Formal Conversations: Meetings, Interviews and Group Discussions: Meetings; Duties of

Participants; Interviews; Group Discussions.

10

Greetings and Introduction: Basics of greetings and introduction; formal and informal

introduction; Reading comprehension, Vocabulary; Pronunciation: Falling and rising tone;

Speaking: Body language; Listening: body language.

11 ListeningSkills:ImportanceofListening;ListeningversustheSenseofHearing;Listening

asBehaviour;PayoffsforEffectiveListening;ActionsRequiredforanEffectiveListener;

Approaches to Listening; Misconceptions and Barriers that Impair Listening; Planning for

Effective Listening; How to be a Good Listener?; What Speakers can do to Ensure Better

Listening?.

12 Formal and Informal Letters: Distinction between Formal and Informal Letters; Writing

Formal Letters; Informal Letters.

13 Communication on the Net: E-Mail; Netiquettes; Blog Writing; Web Writing.

14

Report Writing: Business Reports: Significance; Types of Reports; Five Ws and one H;

Report Planning; Report Writing Process; Outline of a Report; Guidelines for Writing Report;

Technicalities of Report Writing; Visual Aids in Reports; Criteria used for Judging the

Effectiveness of a Report; Illustrations.

15 Job Applications and Resume Writing: Job Application/Covering Letter; Resume/CV

Writing.

Course outcomes (COs):

Upon completion of this course, the students will be able to:

1. Improve language proficiency in English.

2. Hone the LSRW skills within and beyond the classroom environment.

3. Integrate English language learning with employability skills.

4. In calculate the habit of speaking in English fluently with observation and practice.

5. Develop skills for creative writing.

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Harvard Business School Press (2003), Business Communication: Harvard Business Essentials,

Boston,Massachusetts.

B. Krizan, A.C. Buddy, Merrier, Patricia, Logan, Joyce and Williams, Karen (2008), Business

Communication, ThomsonSouth-Western.

C. Guffey,m Mary E. (2000), Business Communication: Process and Product, South-Western

College Publishing.;

WEB LINKS:

A. http://www.commissionedwriting.com/GRAMMAR%20ESSENTIALS.pdf.

B. http://www.esf.edu/fnrm/documents/FNRM_Communications_Handbook2008.pdf.

C. Http://books.google.co.in/books?id=RETE15K43qsC&printsec=frontcover&dq=essentials+of+en

glish+grammer+pdf&hl=en&sa=X&ei=XlpSU6PEKY2HrgfyqoDoAQ&ved=0CDIQ6AEwAQ#v

=o nepage&q&f=false.

CELL BIOLOGY

Course Learning Objectives:

a. Describe the properties and functions of the major groups of biochemical.

b. Give an account of the origin of life, from the abiotic world to multicellular organisms, including

an account of endosymbiosis.

c. Give an account of the structure and functions of the plasma membrane and the major organelles

that occur in eukaryotic cells.

Course Detail:

UNIT

CONTENT

1

Cell Structure and Cell Organelles: What is Cell Biology? Significant Events in Cell Biology,

Careers in Cell Biology; Types of Cells, Prokaryotic Cells, Eukaryotic Cell; Plasma lemma or

Cell Membrane, A Historical Perspective, Basic Membrane Architecture, Lipids, Membrane

Polarity, Membrane Skeleton, Carbohydrates, Proteins, Models of the Plasma Membrane,

Mosaic Properties of Cell Membranes: Structure and Functions of Cell Organelles; Nucleus,

History, Structures, Function, Evolution; Mitochondria, Structure, Organization and

Distribution, Functions, Origin; Ribosomes, Structure, Function, Regulation, Structure Linkage,

Function Linkage, Regulation Linkage; Golgi Bodies, Evolution, Discovery, Structure, How

does the Golgi Apparatus Form? Function, Vesicular Transport, Transport Mechanism;

Lysosomes, Enzymes, Functions; Endoplasmic Reticulum, Structure, Rough Endoplasmic

Reticulum, Smooth Endoplasmic Reticulum, Sarcoplasmic Reticulum, Functions; Vacuole,

Bacteria, Plants, Fungi, Animals.

2

Structure of Chromosome: Historical background of chromosome, Number of Chromosomes,

Size of chromosomes; Structure of Chromosome, Chemical Structure of Chromosome,

Molecular Structure of Chromosomes; Euchromatin and Heterochromatin; Types of

chromosome on the basis of centromere position, Karyotype; Functions of Chromosome;

SpecialTypesofChromosomes,LampbrushChromosome,PolyteneChromosomes,B-

Chromosomes

3

Structure of DNA and Types of DNA: Systemic Position of DNA in a cell; History of DNA,

Gregor Mendel, Frederick Griffith, Oswald Avery, Erwin Chargaff, Roslind Franklin and

Maurice Wilkins, James Watson and Francis Crick; DNA is the Genetic Material, The Avery

Macleod Mc Carty Experiment, The Hershey-Chase Experiment; Structure of Nucleic Acid,

Nucleosides, Nucleotides; Components of Nucleic Acids; Differences between Prokaryotic and

Eukaryotic DNA; Molecular structure of Deoxyribonucleic Acid, Deoxyribose, Nitrogenous

Bases, Phosphate; Types of DNA, On the basis of Number of Strands, On the Basis of

Nucleotide Residues, On the Basis of Shape, On the Basis of the Nature of Nucleotide Sequence

in Duplex DNA; Properties of DNA, The Size of DNA Molecule, Denaturation, Fragility of

DNA Molecule, Renaturation, Effect of pH on DNA, Stability, Hyper Chromic Effect;

Functions of DNA, Chemistry of DNA, Double-Helical DNA and RNA can be Denatured,DNA

Use in Technology

4

Types of RNA: Molecular structure of RNA; Chemical structure of RNA; Comparison with

DNA; Strategies for analyzing RNA structure; Synthesis of RNA (Transcription); Types of

RNA, Messenger RNA, Ribosomes and Ribosomal RNA (rRNA), Transfer RNA(tRNA),

Ribozymes, Antisense RNAs, Viral Genomes, Other RNAs; Functions of RNA.

5

Cell Cycle: Mitosis and Meiosis: Cell cycle; Regulation of the Cell Cycle, Regulators of the

cell cycle, Protein Degradation; Cell Cycle Regulation in Development, Cell Cycle Variation,

Embryonic Cell Cycles, Larval Somatic Cell Cycles, Endoreduplication Cycles, Meiotic Cell

Cycle, Checkpoint Control, DNA damage induced Checkpoint, DNA replication induced

Checkpoint, Spindle assembly Checkpoint, Cell Cycle Entry and Arrest; Interphase; Mitosis,

Cytokinesis,SignificanceofMitosis;Meiosis,SignificanceofMeiosis;ComparisonofMitosis

and Meiosis; Gametogenesis, Spermatogenesis, Oogenesis, Significance of DNA

6

DNA Replication: DNA Replication: An overview; DNA polymerase; Central Dogma

Statement, Overview, DNA; Replication process; Transcription, Initiation, Elongation,

Termination; Translation, Activation, Initiation, Elongation, The Mechanics of itall.

7

DNA Repair: DNA Damage and Repair Mechanisms; Sources of DNA damage; Types of DNA

damage; Mechanisms of DNA Repair; Global response to DNA damage, DNA Damage

Checkpoints, Prokaryotic SOS Response, Eukaryotic Transcriptional Responses to DNA

Damage; DNA Repair and Aging, Pathological Effects Poor DNA Repair, Longevity and

Caloric Restriction

8

Cell Adhesion: Cell adhesion: An overview, Physical Connections between Cells, Forming the

Connections between Cells; Process in Eukaryotes and Prokaryotes, Eukaryotes, Prokaryotes;

Differential adhesion hypothesis, Background, Overview, Applications; Clinical Implications of

Cell Adhesion.

9

Cell Biology Laboratory Manual: Microscope, Aberrations, Angle of Incidence, Alignment,

Bright Field, Dark Field and Phase Contrast; Types of Microscope, Electron Microscope,

Scanning Electron Microscope; Histochemistry, Fixation, Dehydration, Embedding, Paraffin,

Plastic, Sectioning, The Ultramicrotome, The Cryostat; Cell Fractionation, Homogenization,

Osmotic Alterations, Mortars and Pestles, Blenders, Compression/Expansion, Ultrasonification,

Gravity Sedimentation, Centrifugation, Physical Properties of Biological Materials,

Sedimentation Velocity, Sedimentation Coefficient, Diffusion Coefficient, Sedimentation

Equilibrium; Electrophoresis, Cationic vs. Anionic Systems, Tube vs. Slab Systems,

Continuous vs. Discontinuous Gel Systems, Agarose Gels; Cell Cycles, Interphase G1-S-G2,

Prophase, Metaphase, Anaphase, Telophase, Meiosis, Prophase-I: Leptotene 1, Prophase I:

Zygotene,ProphaseI:Pachytene,ProphaseI:Diplotene,ProphaseI:Diakinesis,Metaphase-I,

Anaphase-I, Telophase-I: Interphase, Prophase-II: Telophase II, Damage Induced during

Division; The central dogma.

Course Outcomes (COs):

Upon the completion of the course students will able to

1. Describe the cell structure, components of cell, enzymes to emphasize the importance of cell as the

basic unit of an organism.

2. An understanding about the role of various cellular organelles in modifying the functions of the

cells, especially, metabolism and protein synthesis.

3. The role of cytoskeleton and modes of cellular transport will be discussed.

4. Understanding the cellular regulation through various types of cell signaling, cell division,

apoptosis and cell differentiation.

5. Provide an overall understanding of the epithelial cells and cancer with a focus on neurobiology

and neurodegenerative diseases.

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Cell Biology, Third Edition, By S C Rastogi,2005

B. Cell Biology, By Melissa Stewar,2008

C. Molecular Biology, By David P. Clark, Nanette Jean Pazdernik,2013

D. Lodish, Harvey, et al. (2003) Molecular Cell Biology 5th Edition. W. H. Freeman,pp.659-666.

WEB LINKS:

A. http://biology.unm.edu/ccouncil/Biology_124/Summaries/Cell.html

B. http://biologyclc.uc.edu/courses,bio104/cells.htm

C. www.edu.pe.ca/gray/class_pages/rcfleming/cells/notes.htm

CELL BIOLOGY (P)

1. Microscopic Examination of Cells

2. Dilution Techniques

3. Measurement of Solutes

4. Sampling and Isolating Bacteria

5. Staining and Counting Bacteria

6. Physiological Processes of Bacteria

7. Comparison of Normal and Transformed cells

8. Mitosis &Meiosis

9. Inheritance

10. Analysis of Proteins by Chromatography and Electrophoresis

BIOINFORMATICS

Course Learning Objectives:

a. To impart knowledge on basic techniques of Bioinformatics Course Outcome

b. At the end of the course, the students would have learnt about Sequencing Alignment and

Dynamic Programming, Sequence Databases, Evolutionary Trees and Phylogeny at elementary

level.

Course Detail:

UNIT

CONTENT

1

Introduction to Bioinformatics: Definition of Bioinformatics; Aims of Bioinformatics;

Applications of Bioinformatics, Sequence Alignment, Multiple Sequence Alignment; Prediction

of RNA Secondary structure; Protein secondary structure prediction; Microarray, Types of

Microarrays; Computer added drug designing, Pharmacogenomics, Evolutionary Analysis.

2

Biological Databases: Databank, Database; Classification of Biological Database; Types of

Database, Sequence Databases, Macromolecular Structure Database, Proteomic Databases,

Protein Sequence Databases, Structure Database, Conserved Domain Database, Interaction

Databases,MINT,RNADatabase,GeneExpressionDatabases,OntologyDatabases;Database

of genetic and proteomic pathways, Expression, Regulation and Pathways Databases, KEGG

Pathway Clinical Databases, Microarray Databases; Literature database, PubMed, PubMed

Central, OMIM, Bookshelf, List of other Biological Databases, Types of Biological Databases:

At NCBI

3

Phylogenetic Analysis: Fundamental elements of phylogenetic models; Tree interpretation-The

Importance of Identifying Paralogs and Orthologs; Phylogenetic data analysis: The Four Steps,

Alignment: Building the Data Model; How much Computer dependence, Phylogenetic Criteria

Preferred, Alignment Parameter Estimation, Mathematical Optimization and Analysis of

structures, Alignment: Extraction of a Phylogenetic Data Set, Determining the Substitution

Model, Which Substitution Model to Use; Tree Building methods, Distance based Methods,

Unweighted Pair Group Method with Arithmetic Mean (UPGMA), Neighbor Joining (NJ), Fitch

Margoliash (FM), Minimum Evolution (ME), Character based Methods, Maximum Parsimony

(MP), Maximum Likelihood (ML); List of some Specific software for phylogenetic analysis,

PHYLIP, MEGA, VOSTORG, COMPROB, PAUP, MARKOV Puzzle; Phylogenetic Activity,

Exercise 1: Relatives of Relatives, Exercise 2: Understanding Historical Relationships, How did

You Do? Exercise 3: Comparing Trees, Exercise 4: Multiple Sequence Alignment; DNA

sequencing; Protein Sequencing, Hydrolysis, Separation, Quantitative Analysis, N-terminal

Amino Acid Analysis, C-terminal Amino Acid Analysis, Edman Degradation, Mass

Spectrometry, Importance of Sequencing.

4

Application of Bioinformatics Websites: Website, Static Website, Dynamic Website;

Computers in biochemical research, Biochemical Computers, Biomechanical Computers,

Bioelectronic Computers; Data collection; Data storage, Hierarchy of Storage; National centre

for Biotechnology information (NCBI 2001), Path to the Bioinformatics, Role of

Bioinformatics, Applications of Bioinformatics; Cheminformatics and drug design, Molecular

Phylogenies; Partnership in bioinformatics, Importance of databases; Types of databases; What

is GenBank?, Updating or Revising a Sequencing a Sequence, New Developments; EMBL,

EMBL Nucleotide Sequence Database; Biological annotation, Data Distribution Searching and

Sequence Analysis; EMBnet, Citing the EMBL Database; DDBJ, Specialized Databases

Developed at DDBJ, Uniprot; Derived database, Using a WHERE Clause to Specify Selection

Conditions; MySQL, Installing the MySQL DBMS, Setting up MySQL, Using the MySQL

Client Program, Using the MySQLadmin Client Program to set up MySQL, safe_MySQLd and

Securing your MySQL Server; Steps of Model designing, Template and Sequence Alignment,

Fragment Assembly, Segment Matching; Satisfaction of Spatial restraints, LoopModelling;

Sequence alignment, Interpretation, Alignment Methods, Representations; Global and Local

Alignments; BLASTA and FASTA.

5

Homology Modeling: What is Homology?, General Procedures; PAM Matrices, BLOSUM

Matrices; Identification of structurally conserved and structurally variable regions, Generating

Coordinates for the Unknown Structure; Evaluation and refinement of the structure, Class-

Directed Structure Determination; Steps in model production, Model Generation; Structural

comparison methods, Benchmarking, Accuracy, Sources of Error.

6

Drug Designing: What is in silico drug design?, Why in silico drug design is significant?; Drug

discovery methods, Types; Major steps in the drug design process, Find What is Known,

Develop and Assay, Consider Financial Issues, Find Lead Compounds, Isolate the Molecular

basis for the Disease, Refine Drug Activity, Drug Testing, Formulation, Production, Marketing,

Non Prescription Sales, Genetic Production; Drug designing steps, Other Sites.

7

Networking and Website: Communication models; Protocols; Basic network terminologies,

Bridges, Routers, Switches, Gateways, Hubs, Content Filters, Firewalls, Modems, Satellites;

Network interface cards, Network Monitors; Security, Antiviral Utilities, Authentication,

Firewalls, Encryption, Cryptography; Databases.

Course Outcomes (COs):

Upon the successful completion of the course, students will able to

a) Infer the biological problems using appropriate in silico approaches.

b) Select the suitable tools or servers to solve the specific biological issue and curate experimental

data.

c) Perform and analyze database similarity search and sequence alignment.

d) Construct and analyze phylogenetic trees.

e) Use appropriate tools and packages to analyze varied range of biological problems.

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Jeremy Ramsden-2009, Bioinformatics: An introduction, SecondEdition.

B. Brown TA. Oxford: Wiley-Liss; 2002, Second Edition,Genomes.

C. Michael M. Miyamoto, Joel Cracraft-1991, Phylogenetic Analysis of DNASequences.

D. Mohammed J. Zaki, Christopher Bysroff-2008, Protein structureprediction.

WEB LINKS:

A. http://www.informit.com/articles/article.aspx?

B. http://www.rackspace.com/information/hosting101

C. http://compnetworking.about.com/od/basicnetworkingconcepts/

BIOINFORMATICS (P)

1. Retrieve the protein or DNA sequence and convert it into FASTAformat

2. Find out the similarity search of unknown protein sequence using BLAST

3. Find out the similarity search of unknown protein sequence using FASTA

4. Open Reading Frame prediction for different protein out of some given nucleotidesequences

5. Gene finding related search for a given nucleotide sequences in order to predict the Gene

6. Secondary structure prediction for Amino acid sequence of a given protein

7. Predict and visualize the 3D structure of any protein

8. Prepare sequence file in FATSA format and multiply, align them using web based CLUSTALW

9. Molecular modeling using Modeler Software

10. Docking studies using Auto dock Software

BIOMOLECULES

Course Learning Objectives:

a. Discuss the elementary biochemistry of the molecules of life and describe the relationship

between the structure and function of biomolecules..

b. Compare the structure and function of cells from different domains.

Course Detail:

UNIT CONTENT

1

Bimolecular: An Overview: Structure and Functions of Bio molecules, Diversity and

Distribution of Bimolecular; General Introduction of composition of living matter; Cell wall

structure.

2

Carbohydrates: Carbohydrate nomenclature; Monosaccharides, Classification of

Monosaccharide, Properties of Monosaccharide, Chemical Properties of Monosaccharide,

Derivatives of Monosaccharide, Glycosidic Linkage, Biological Significance of

Monosaccharide; Oligosaccharides, Disaccharides, Higher Oligosaccharides; Polysaccharides,

Homo polysaccharide, Hetero polysaccharides, Glycosaminoglycans,Glycoconjugates:

proteoglycans, glycoproteins and glycolipids, Biological functions of carbohydrates,

3

Lipids: Fatty acids, Saturated and Unsaturated fatty acids, Naming of Fatty acids; Saturated and

Unsaturated Fats, Sources of Saturated and Unsaturated Fats, Essential Fatty acids;

Classification of lipids, Simple lipids, Compound lipids, derived lipids; Biologically important

cholesterolderivatives,Fatsolublevitamins,Eicosanoids,Lipoproteins,Biologicalfunctionsof

Lipids, Cellular Energy Source, Storage of Triglyceride in Adipose Cells, Mobilization of Fatty

Acids, Membrane Component.

4

Amino Acids: Amino Acids: An Overview; Functions of Amino Acid; Some Important Amino

Acids, Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine,Threonine,

Tryptophan, Valine, Non-essential Amino Acids

5

Proteins: Classification of proteins on the basis of shape and solubility, Simple and Globular

Proteins, Conjugated Proteins, Derived Proteins; Biological functions of proteins; Composition

of Proteins, α-Amino acids, Properties of Amino Acids, Standard Amino Acids, Essential and

Non essential Amino Acids, Titration of Amino Acids, Absorption of UV- light by Aromatic

Amino Acids, The Peptide Bond; Overview of Protein Structure, Primary, Secondary, Super

secondary, Fibrous Proteins and Tertiary Structure

6

Nucleic Acids: The chemical composition of nucleic acids, Nitrogenous Bases, The Pentoses of

Nucleotides and Nucleic Acids, Nucleosides, Nucleotides, Polynucleotides; Structural

Organization of Nucleic Acid, Chargaff’s Rule; Classes of Nucleic Acids; Deoxyribonucleic

Acid (DNA), Structure of Double stranded DNA, Features of B form of DNA (Watson-Crick

Model), Alternative Forms of DNA, DNA Topology, Denaturation, and Renaturation of DNA,

Biological Significance of DNA; Ribonucleic Acid (RNA), Structure of Ribonucleic Acid, The

Primary Structure of RNA, Types of RNA, Regulatory RNAs, Comparison between DNA and

RNA

7

Enzymes: Properties of Enzyme; Nomenclature of Enzyme; Major Classes of Enzymes;

Enzyme Action, Unit of Enzyme Activity, Turnover Number, Enzyme Specificity, Catalytic

Mechanism of Enzyme Action; Enzyme Kinetics, Michaelis-Menten Approach to Enzyme

Kinetics, Steady State Assumption, Line Weaver-Burk Plot or Double Reciprocal Plot,

Significance of Km and Vmax Values; Significance of Kcat, and Kcat/Km; Factors Determines the

Rate of an Enzymatic Reaction, Effect of substrate concentration, Effect of enzyme

concentration, Effect of Temperature, Effect of pH, Effect of Inhibitors, Effect of Activators;

Enzyme Inhibition, Allosteric Enzymes, Isoenzymes, Zymogens, Lysozymes; Regulation of

Enzyme Activity, Reversible and Irreversible Covalent Modification, Regulation of Activity by

Anchoring of Enzymes in Membrane: Spatial relationship, Regulation of Activity by Enzyme

SynthesisandDegradation,RegulationofActivitybyothermeans:Specializedcontrol,

Regulation of Activity by Feedback Inhibition, Other Regulatory Mechanisms

8 Vitamins: Vitamins: An Overview; Types of vitamins, Water soluble Vitamins, Fat soluble

Vitamins; Importance of vitamins; Applications of all types of vitamins.

Course Outcomes (COs):

Upon the successful completion of course, the students will able to

a) Provide basic understanding of carbohydrates, lipids, and proteins and their roles in normal

biological processes

b) Metabolic pathways of carbohydrates along with their roles in providing energy will be discussed

in detail and

c) Knowledge about the structural units of proteins, amino acids, and their metabolism will be given

d) Information about fatty acids and its metabolism and the structural units of genetic code will be

provided

e) Cellular processes involved in the generation of energy will be discussed in detail

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Voet&Voet Text Book of Biochemistry, 3rd

Edition

B. Lehninger, Principles of Biochemistry, 4thEdition

C. Charles M. Grisham, Biochemistry: ReginaldGarret

D. Hiram F. Gilbert, Basic Concept in Biochemistry: A Student SurvivalGuide

WEB LINKS:

A. http://www.worhington-biochem.com/introbiochem/enzymes.pdf.

B. http://courses.chem.psu.edu/chem112/materials/enzymes.pdf.

C. http://www.biologymad.com/resources/Ch%204%20-%Enzymes.pdf.

BIOMOLECULES (P)

1. Preparation of Solutions

2. Preparationbuffer

3. Estimate the concentrations of reducing sugar present in given sample by DNSAmethod

4. Estimate the concentrations of sugar present in given sample by Anthronemethod

5. Estimate the concentration of amino acids in given sample by Ninhydrinmethod

6. Estimate the concentration of protein in given sample by Biuretmethod

7. Estimate the concentration of protein in given sample by Folin-Lowry’smethod

8. Estimate the concentration of protein in given sample by Bradford’smethod

9. Estimate the amylase activity present in the givensample

10. Investigate the effect of temperature on amylase activity and find out the temperature optima for

amylase.

PLANT BIOCHEMISTRY

Course Learning Objectives:

a. To provide comprehensive information on the fundamentals of Biochemistry.

b. To provide an in-depth understanding on the origin and history of Biochemistry.

c. To give a detailed knowledge of basic biomolecules such as carbohydrates, proteins, lipids etc.

d. It also provides a deep understanding on some basic cellular processes such as photosynthesis,

photorespiration, nitrogen fixation etc.

Course Details:

UNIT

CONTENT

1

Basic Biochemistry and Bio-molecules: Scope and importance of biochemistry and molecular

biology in plants; Structural organization of prokaryotic Cells, Internal Structure of Prokaryotic

Cells, Genetic Materials of Prokaryotes, Prokaryotic Cell Structures Outside of Plasma

Membrane; Structural Organization of Eukaryotic Cells, Internal Membrane, Mitochondria and

Plastids, Cytoskeletal Structures, Cell Wall, Plant Cell; Virus: Structural Organization,

Icosahedral, Envelope, Complex, Bacteriophage, Helical; Fractionation of Plant Cell

Organelles; Chemical Bonding in Biological Systems, Entropy and the Laws of

Thermodynamics, Protein Folding can be Understood in Terms of Free Energy Changes,

Biological Buffer and pH; Redox Reactions, Reactions during Photosynthesis, Location of the

Redox Reactions in the Plants; Role of High Energy Phosphates, High energy Compounds,

Representations of High energy Phosphate Bonds; Biomembranes, Phospholipids, Cytosolic and

an Exoplasmic Face, Phospholipid Composition Differs in Two Membrane Leaflets;

Carbohydrate, Classification of Carbohydrates, Structure and properties of Carbohydrates,

Functions of Carbohydrate; Proteins, Classification, General Structure and properties of

proteins, Protein Functions; Lipids, Classification of Lipids, Structure of Lipids, Properties of

Lipids, Functions of Lipids; Nucleic Acids, Types and Structure of Nucleic Acids, Biochemical

Properties of Nucleic Acid, Biological Role of Nucleic Acids; Prostaglandins, Structureof

Prostaglandin, Functions of Prostaglandins.

2

Intermediary Metabolism: Anabolism, Carbon Fixation, Carbohydrates and Glycans, Fatty

Acids, Isoprenoids and Steroids, Proteins, Nucleotide Synthesis and Salvage; Catabolism,

Energy from Organic Compounds, Digestion; Metabolism of Carbohydrates, Glycolitic

Pathway, Hexose Monophosphate Shunt Pathway, Tricarboxylic Acid Cycle, Glyoxylate Cycle,

Gluconeogenesis; Biological Oxidation, Electron Transport Chain Makes Energy, Oxidative

Phosphorylation; Lipid Metabolism, Energy Production Fatty Acid Oxidation; Amino Acid,

Glutamate family, Aspartate Family, Alanine-valine-leucine Group, Aromatic Amino Acids;

Metabolism of Nucleic Acids, Formation of PRPP, DE NOVO Ribonucleotide Synthesis,

NucleotideCatabolismandSalvage;OverallMetabolism;SignalTransductionMechanisms,

Role of Ion Channels in ABA Signaling, Light-induced Stomatal Opening, ABA-induced

Stomatal Closing.

3

Biochemistry of Food-grains, Fruits and Vegetables: Fundamentals of Nutrition, Major

Nutrients; Concept of Balanced Diet, Factors Determining Food Acceptance/choice,

Regulations of Body Temperature, Recommended Dietary Allowances (RDA) for Average

Indian; Physiology and Nutrition of Carbohydrates, Fats and Proteins, Carbohydrates, Fats,

Proteins; Vitamins, Classification of Vitamins; Biochemical Composition and Food Value,

Pulses, Cereals and Whole Grains, Oilseeds, Fruits and Vegetables; Biochemistry of Fruit

Ripening,PostharvestBiochemicalChanges;StorageofFruitsandVegetables,Methodsof

Preservation,OtherFactorstoConsider;BiochemicalBasisofQualityImprovement,Enzymic

Changes, Chemical changes, Physical Changes, Biological Changes, Methods of Reducing

Deterioration; Antioxidants, Reactive Oxygen Species, Antioxidant protection, Dietary

Antioxidants, Phytonutrients, Endogenous Antioxidants; Nutraceuticals, Classification of

Nutraceuticals, Dietary Supplements, Functional Foods; Food Toxins, Natural Toxins present in

Food of Plant Origin, Natural Toxins present in food of animal origin, Toxic Effects and Food

Poisoning, Risk Reduction Measures; Antimetabolites; Food Additives, Categories, Safety;

Storage Proteins.

4

Photosynthesis: Photosynthetic Pigments, Pigment Involved in Photosynthesis; Light Reactions

of Photosynthesis, Photo system, Photophosphorylation; Dark Reactions of Photosynthesis, C3

Cycle, C4 Cycle, Crassulacean Acid Metabolism; Carbon Cycle; Photorespiration;

Photosynthesis, Photorespiration and Crop Productivity; Chloroplast, Structure, Biochemical

Anatomy, Interaction between Chloroplast, Cytosol and Other Cell Organelles; Seed Reserve

Biosynthesis, CWSPs in Endosperms, CWSPs in Cotyledons.

5

Plant Metabolic Processes: Metabolism of mineral nutrients in plants; Sulphur metabolism,

Sulphate Assimilation in Lower Plants and Algae, The Need to Adapt to and Manage Sulphur

supply; Nitrogen cycle, Nitrogen Fixation, Nitrification, De-nitrification, Nitrate and Nitrite

Reduction; Biochemical and physiological role of hydrogenase, Structural Classification,

Biological Function, Physiological Role; Chemoautotrophy in Rhizobia and Nitrifying bacteria,

Oxidation of Ammonia to Nitrate; Cell cycle; Growth regulation in plants, Three Common Plant

Growth Regulators, Plant Growth Regulators and Food Safety; Signal transduction and

phytohormones, The shade Avoidance Response; Molecular mechanisms of plant Growth,

Hormone action, Perception and Signal Transduction; Role of oligosaccharides and

polysaccharides in cellular metabolism, Metabolism of cyanogenic glycosides and

glucosinolates.

6

Plant Molecular Biology: Plant Genome Organization, Plant Nuclear Genome, Chloroplast

Genome Organization, Mitochondrial Genome Organization; Genomics, Functional Genomics;

Tissue Specific Expression of Genes; Molecular Biology of Various Stresses, Molecular

Biology of Drought, Salinity Stress and Plant Response; Signal Transduction and its Molecular

Basis, Molecular Mechanism of Plant Hormone Action; Structure, Organization and Regulation

of Nuclear Genes, Composition of Nuclear DNA, Genome Size or Nuclear DNA Content;

Genes Involved in Nitrogen Fixation; Regulation of Chloroplast Gene Expression;

Mitochondrial Control of Fertility, Genes and Genetic Capacity, Cytoplasmic Male Sterility;

PlantMolecularMarkersandtheirApplications,DNAbasedMolecularMarkers,Properties

Desirable for Ideal DNA Markers, Types and Description of DNA Markers, Applications of

Molecular Markers in Plant Genome Analysis and Breeding.

7

Plant Biotechnology: Totipotency; Application of tissue culture for plant improvement, Plant

Breeding and Biotechnology, Wide Hybridization, Haploids, Somaclonal Variation, Micro

propagation; Cryopreservation, Methods of Cryopreservation of Plant Genetic Resources;

Principles of Gene Cloning; Isolation and Characterization of Plant Genes; Gene Transfer,

Target Cells for gene transformation, Vectors for gene transfer, Gene delivery Methods; Gene

Silencing; Site-directed Mutagenesis.

Course Learning Outcomes (COs):

a. Provide basic understanding of carbohydrates, lipids, and proteins and their roles in normal

biological processes.

b. Metabolic pathways of carbohydrates along with their roles in providing energy will be discussed

in detail.

c. Knowledge about the structural units of proteins, amino acids, and their metabolism will be given.

d. Information about fatty acids and its metabolism and the structural units of genetic code will be

provided.

e. Cellular processes involved in the generation of energy will be discussed in detail.

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

D. Principles of Biochemistry, Donald Voet, Charlotte W. Pratt, Judith G. Voet,2013

E. Lea PJ &Leegood RC. 1993. Plant Biochemistry and Molecular Biology.2nd

Edition JohnWiley.

F. Heldt HS. 1997. Plant Biochemistry and Molecular Biology. Oxford Univ.Press.

G. S.R. Mishra (2003)Biomolecules.

WEB LINKS:

D. http://www.biochemj.org/bj237/0001/237001.pdf.

E. http://www.springer.com/life+sciences/journal/13562

F. http://en.wikipedia.org/wiki/biochemistry

G. http://www.sciencedirect.com/science/book/9780122146749

ENZYMOLOGY

Course Learning Objectives:

a. To plan and execute an enzyme assay;

b. To analyse enzyme kinetic data;

c. To analyse kinetic inhibition data and to determine the mechanism of inhibition;

d. To perform library research on a specific enzyme topic.

Course Detail:

UNIT CONTENT

1

Introduction to Enzymes: Theory of Enzyme, What Types of Enzymes are there? How are

Enzymes used? How are Enzyme Preparation made? What Affects the Activity and Stability of

Enzyme?; Classification of Enzymes, General Principles, Common and Systematic Names,

Scheme for the Classification of Enzymes and the Generation of EC Numbers, Rules for

Classification and Nomenclature, Rules and Guideline for Particular Classes of Enzymes;

Protein and Non protein Enzymes; General Properties of Enzymes; Factors Affecting Enzyme

Activity, Effect of pH, Effect of Temperature on Enzyme Activity, Temperature Optimum of an

Enzyme, Substrate Concentration; Catalystic Reaction of Enzyme; Advantages of Enzyme.

2

In Vitro Enzyme Activity: In Vitro Activity of Purified enzymes and their applications in

industry, Specific Activity; Enzyme uses in food processing, medicine Diagnostics and

production of new compounds, Food Processing Medical Applications of Enzymes, Diagnostics,

Production of New Compounds, Other Application; Enzymes as research tool, Alcohol

Dehydrogenase (ADH), Malate Dehydrogenase (MDH), Lactate Dehydrogenase (LDH);

Modification of biological compounds with the help of enzyme; Enzymes in MolecularBiology.

3

Enzyme Kinetics: Basic definitions, Rates of Consumption and Formation, Rate of Reaction,

Elementary and Composite Reactions, Order of Reaction and Rate Constant, Numbering of

Reactions, Steady state Approximation; Enzyme reactions involving a single substrate, Limiting

Kinetics of Enzyme- Catalysed Reactions; Enzyme reactions involving more than one substrate,

Michaelis-Menten Kinetics; Inhibition, Reversible and Irreversible Inhibitions, Linear and Non

linear Inhibition, Degree of Inhibition, Classification of Inhibition Types, Product Inhibition;

Comparison of Enzyme Kinetics with Radioligend binding, Lineweaver-Burk Plot, Eadie-

Hofstee Plot, Hanes-Woolf Plot; Enzyme Inhibitors, Non-specific Inhibitors, Competitive

Inhibitors; Rapid Kinetics, Stopped-Flow, Quench-Flow.

4

Enzymes Metabolism: Molecular Recognition, “Lock and Key” Hypothesis, “Induced Fit”

Hypothesis; Stabilization of the transition state, Enzymes supply Enormous Rate Accelerations;

Entropy loss and destabilization of the ES complex, Transition State Analogs Bind Very Tightly

to the Active Site; Types of Enzyme catalysis, Covalent Catalysis, Base Catalysis, Metal Ion

Catalysis; Enzyme mechanisms, Serine Proteases, Aspartic Proteases, AIDS Virus HIV-1

Protease, Lysozyme; Allosteric interaction, Models of Allosteric Regulation, Historic Examples

ofCooperativity and Allostery in Proteins, Types of Allosteric Regulation.

5

Special Enzymes: Metal Ions; Organic cofactors, Vitamins and Derivatives; Cofactors as

Metabolic intermediates, Isozymes, Metalloenzyme; Function and role, General Functions of

Metalloenzymes; Regulation and control, Metalloenzyme Inhibition, Membrane Bounded

Proteins; Different methods of enzyme extraction, Enzyme Activities Assay, Preparation of the

Reagents; Lipid protein interaction.

6

Immobilization: Immobilization of Enzymes; Kinetics of immobilized enzyme; Effect of solute

partition on the kinetics of immobilized enzyme; Effects of solute diffusion on the kinetics of

immobilized enzymes, Applications of immobilized enzymes, Use in Medicine, Therapeutic

Uses, Using Enzyme Inhibitors, Other uses.

Course Outcomes (COs):

Upon the successful completion of the course, students will able to

a) To understand the IUBMB system of enzyme classification.

b) To learn the factors involving and factors affecting the enzyme activity.

c) To learn the kinetics of single and multi enzyme substrate enzyme catalysed reaction Know to solve

the problems based on single and multi substrate reactions

To understand the analytical techniques available for enzyme analysis

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Koshland D. The Enzymes, v. I, ch. 7, Acad. Press, New York,1959

B. Donald Voet, Judith Voet and Charlotte W Pratt. Fundamentals of biochemistry, life at

molecular level. 2nd

Edition, John Wiley2006

C. Trevor Palmer. Enzymes: biochemistry, biotechnology and clinical chemistry. East West Press

2004

WEB LINKS:

A. http://www.sciencedirect.com/science/bookseries/00766879

B. http://www.biochem.med.umich.edu/?q=enzymology

C. http://en.wikipedia.org/wiki/Methods_in_Enzymology

D. http://www.thefreedictionary.com/enzymology

YEAR-II

INSTRUMENTATION AND TECHNIQUES

Course Learning Objectives:

a. To introduce students to the use of basic biological research instrumentation

b. To develop the laboratory skills and techniques required to design experimental protocols and test

hypotheses utilizing basic laboratory research equipment

c. To develop and improve scientific writing and oral communications skills based upon laboratory

experiences and ability to think critically.

Course Detail:

UNIT

CONTENTS

1

Introduction to Separation Techniques: Centrifugation, Analytical/Preparative

Centrifugation, Ultracentrifugation / Low Speed Centrifugation, Moving Boundary / Zone

Centrifugation, Basic Theory of Sedimentation; Electrophoresis, Gel Electrophoresis,

Understanding Isoelectric Focusing; Chromatography – Basic Operation, Different Types of

Chromatography Methods, Theory of Chromatography, Ion & MoleculeExchange

Chromatography, Instrumental Components

2

Basic Separation Techniques: Immobilized Metal Ion Affinity Chromatography, Recombinant

Proteins; Lectins; Electrophoresis, Theory, Electrophoresis Apparatus being used to Separate

Proteins by Molecular Weight ,Instrumentation, Detection, Modes of Separation, Efficiency and

Resolution, Related Techniques; Paper Electrophoresis; Iso Electric Focusing

3

Microscope: Invention of Glass Lenses, Birth of the Light Microscope, Light Microscope, Parts

of Microscope and their Specifications; Microscopy, Electron Microscopy, Transmission

Electron Microscope (TEM), Scanning Electron Microscope (SEM), Phase Contrast

Microscopy, Confocal Microscopy: Fluorescence: X-ray Crystallography, X-rays and the

Production of X-rays, Continuous and Characteristic X-ray Spectra, X-ray Diffraction and

Bragg’s Law, X-ray powder Method; Radioactivity, Radioisotopes, Radioactive Decay, Nuclear

Reaction, Writing a Nuclear Reaction Equation, Radioactive Decay and Half Life, Carbon

Dating;ScintillationCounter,ScintillationCounterApparatus,LiquidScintillationCounting,

Counting Liquid, Counting Vials, Liquid Scintillation Spectrometry: External Factors

Interfering with β-decay Detection by LSC, Optical CrossTalk

4

Advance Spectroscopy: Spectroscopy, What Do Photo biologists Use Spectroscopy For?, What

Spectroscopy are Available to the photo biologist?; Photo thermal Techniques, Time-resolved

vs. Steady-state Techniques, Ground-state Absorption; Transient Absorption, The pump-and-

Probe Approach, From Milliseconds to Hours; Steady-state Spectrophotometers, From

Milliseconds to Nanoseconds: Nanosecond Laser Flash Photolysis, Sub-nanosecondDomain:

The Two-pulse pump-and-Probe Technique, Emission Spectroscopes; Steady –state Emission

Spectroscopy, Time-resolved Photo acoustics, Photorefractive Techniques, ESR and NMR

Spectrometers: Nuclear Magnetic Resonance Spectrometer, Continuous Wave NMR

Instruments, Fourier Transform NMR Instruments, Microtomy; EPR Spectroscopy, Theory,

Experimental Apparatus; Circular Dichroism (CD) Spectroscopy, Physical Principles of CD,

Secondary Structure from CD Spectra, CD of Peptides

5

Atomic Spectroscopy: Spectrophotometer, UV Spectrophotometer, IR Spectrophotometer, UV

Vis Spectrophotometer; Densitometry Scanner, Differential Scanning Calorimeter, Atomic

Absorption Spectroscopy; Instrumental Details, Light Source, Atomizer, Light Separation and

Detection, Isoelectric Focusing, Ampholytes; Isotachophoresis,Basic Principle of

Isotachophoresis; Requirements of Isotachophoresis, Buffer Additives, Hydrogen Bonding

Agents,Surfactants,SDS is the Detergent Most Commonly Employed in Protein Electrophoresis,

Reducing Agents; Beer-Lambert Law, Instrumentation, Derivation of the Beer-Lambert Law,

Limitations of the Beer-Lambert Law; Horizontal and Vertical Gel Systems, The Horizontal Gel

System, Casting a Horizontal Agarose Gel, Slab Gels

6

Application of Spectroscopy: Application of Spectroscopy in Various Fields; Applications of

UVV is Spectroscopy; Applications of Infrared Spectroscopy, Biological Applications,

Industrial and Environmental Applications; Applications of Circular Dichroism (CD)

Spectroscopy,Instrumentations,BiologicalMolecules;ApplicationsofNuclearMagnetic

Resonance (NMR)Spectroscopy

7

Applications of Chromatography: Application of Chromatography in Various Fields, Test for

Homogeneity of Substances Liable to Contamination with Chemically Similar Substances,

Identification of Pharmaceutical Substances and Preparations, Determination of the Individual

Components of Complex Mixtures or of Substances in Dilute Solution; Application of Paper

Chromatography; Application of Affinity Chromatography, Biomolecules Purified by Affinity

Chromatography, Current Techniques involving Affinity Chromatography, immunoglobulin

Purification (Antibody Immobilization), Recombinant Tagged Proteins, Protein A, G, and L

Purification, Biotin and Biotinylated Molecules Purification, Affinity Purification of Albumin

and Macroglobulin Contamination, Lectin Affinity Chromatography; Application of Gel

Filtration Chromatography, Fractionation by Size, Separation of Monomers from Dimers and

Higher Aggregates, MW Estimation, Native and Others Forms, Determination of Molecular

Weight Distribution of Polymers, Determination of Equilibrium Constants; Applications of Ion

Exchange Chromatography, In the Laboratory, In Industry and Medicine

8

Application of Centrifugation: Applications of Centrifugation in Different Processes;

Applications of Micro centrifuge; Applications of Ultracentrifuge, Types of Ultracentrifuges;

Clarification and Stabilization of Wine

9

Application of Electrophoresis: Applications of Electrophoresis in Various Fields; Application

of Affinity Electrophoresis, Capillary Electrophoresis; Applications of Dielectrophoresis;

Applications of Electrophoresis; Applications of Electro focusing; Applications of Gel

Electrophoresis; Applications of Immunoelectrophoreses; Applications of Isotachophoresis;

Applications of Pulsed Field Gel Electrophoresis

Course Outcomes (COs):

Upon the successful completion of the course, students will able to

a) Explain the basic principles of analyses and detection systems involved in photometric,

fluorometric and luminescence -based methods.

b) Explain principles of electrophoresis and immunochemical techniques and discuss how these

techniques can be used in molecular medicine.

c) Discuss the use of enzyme kinetics in analytical methods.

d) Explain basic principles for chromatographic separation techniques.

e) Discuss quality control, error sources, documentation and storage of experimental data.

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Wootton, David. Bad medicine: doctors doing harm since Hippocrates. Oxford: Oxford

University Press: 2006

B. Knoll, Max. “Aufladepotentiel and SekundaremissionelektronenbestrahlterKorer”. Zeitschrift

fur technischePhysik 16:467-475.1935

C. Harrison, Roger G., Todd, Paul, Rudge, Scott R. Petrides D.P. Bioseparations Science and

Engineering. Oxford University Press,2003

D. Holladay LA. “Simultaneous rapid estimation of sedimentation coefficient and molecular

weight”. Biophys Chem. 1980, 11(2)Pubmed.

WEB LINKS:

A. http://www.lenntech.com/library/clarification/centrifugation.htm.

B. http://www.sigmaaldrich.com/content/dam/sigma-

aldrich/docs/Sigma-Aldrich/Brochure/1/biofiles_v6_n5.pdf.

C. http://www.westfalia-separator.com/applications/beverage-technology/wine/winemaking.html.

MOLECULAR GENETICS

Course Learning Objectives:

a. It is meant to provide a foundation in the field of Genetics that will be important for the

Topics covered in many of the more advanced courses

Course Detail:

UNIT

CONTENTS

1

Nucleic Acid: Chemical Basis of Heredity; Bacterial Transformation Experiments, Griffith

Experiment, Avery, Colin MacLeod and MacLyn McCarty Experiments, Hershey and Chase

Experiment; Deoxyribonucleic Acid (DNA),Genes are made of DNA, Chemistry of DNA,

Structure of DNA, Key Features of DNA Double Helix, Variants of DNA; Structure of

RNA,RNA Content of the Cell

2

Genome Organization: Genome of Organisms, Physical Structure of the Prokaryotic Genome,

Eukaryotic Genome; Repetitive DNA Sequences, Repetitive DNA, Non- Repetitive DNA; Gene

Families, Multigene Families, Simple (Classical) Multigene Families, Complex Multigene

Families; Homologous Genes; Pseudogenes; Mitochondrial an Chloroplast Genome;

Comparison between Prokaryotic and Eukaryotic Genomes

3

Replication of DNA & Chromosome: Replication of DNA, Meselson-Stahl Experiment, Basic

Chemistry of Replication, Enzymes Involved in DNA Replication; Mechanism of DNA

Polymerase, Nick Translation, DNA Polymers in Prokaryotes, Proofreading; Rolling Circle

Replication; Replication of Eukaryotic Chromosome; Eukaryotic DNA Polymerase, Duplication

of Nucleosome, Origin of Replication in Eukaryotes, Eukaryotic Replication Fork, Steps

Involved in the Process of Replication of Eukaryotes; Regulation of Initiation of DNA

Replication; Replication of Heterochromatin Region of DNA, Replication of Telomeric Region

of DNA; Replication of Mitochondrial and Chloroplast DNA

4

Genetic Code and Transcription: Genetic Code; Salient Features of Genetic Code, Codon

Degeneracy, Non-overlapping Nature of Codons, Genetic Code is almost Universal, Genetic

Code is Unambiguous; Transfer of Information via Genetic Code, Reading the Genetic Code

5

Gene Expression and its Regulation: Central Dogma, Major Steps of Central Dogma; Control

of Gene Expression; Principle of Gene Regulation, Regulatory Proteins Involved in Gene

Regulation, Gene Regulation in Prokaryotes, Positive and Negative Gene Regulation,

Regulation of Gene Expression in Eukaryotes, Regulation of Chromatin Modification,

Regulation of Transcription, Regulation of RNA Processing, Regulation of Transportationof

RNAs in to Cytoplasm, Regulation of Translation, Regulation by Signal Transduction

6

Mutation: Discovery of Chromosome; Eukaryotic Chromosome; Structure of a Chromosome;

Morphological Forms of Chromosomes, Nucleolar Chromosomes, Sat-Chromosome;

Chromosome Abnormalities and Karyotype; Variations of the Chromosome Structure;

Variations of the Chromosome Number, Human Abnormalities due to Alterations in

Chromosome Number, Non-disjunction Involving Autosomes, Chromosomal Rearrangements

and Speciation; Chromosomal Theory of Inheritance

7 Gene Interaction: Genetic Linkage; Linked Genes; Types of Linkage, Complete Linkage,

Incomplete Linkage; Arrangement of Genes; Crossing Over, Types of Crossing Over, Types of

Crossing Over, Theories of Crossing Over, Cytological Basis of Crossing Over, Crossing Over

and Linkage Maps; Map Units; Three-Locus Mapping; Interference and Coincidence;

Applications of Genetic Mapping

8

Recombinant DNA Technology: Development of Recombinant DNA Technology, Enzymes

Involved in Recombinant DNA Technology, Restriction Endonucleases; Step Involved in DNA

Cloning, DNA Isolation, Cutting of DNA, Joining DNA, Transfer of Recombinant Plasmid

DNA to a Bacterial Host, Amplification Recombinant DNA, Screening; Different Types of

Cloning Vectors, Plasmid DNA as a Vector, Cloning Vectors Based on Viral DNA, Cloning

Vector Based on λ Phage, Replacement λ Vectors, Insertion λ Vectors, Cosmids, Cloning

Vector Based on M13 Phage, Phagemid Vectors, Yeast Artificial Chromosome (YAC) Vectors;

Methods of Recombinant DNA Technology, Finding the Gene of Interest, Gel Electrophoresis,

Radio labeling, Nucleic Acid Hybridization, Northern and Southern Blotting; DNA Libraries,

DNA Sequencing; Sanger “Dideoxy” DNA Method of Sequencing, Automated DNA

Sequencing, Polymerase Chain Reaction, Expression Vectors, Restriction Mapping; Restriction

Fragment Length Polymorphism (RFLP), RFLPs can Serve as Markers of Genetic Diseases;

Applications of Recombinant DNA Technology, Gene Therapy, Vaccine Production,

Agricultural Applications, Herbicide Resistance, Nitrogen Fixation, Insect Resistance,Farm

Animals

Course Outcomes (Cos):

Upon the successful completion of the course, students will able to

a. Recall and relate the role of genes, genetic code, recombinant methods in DNA technology.

b. Describe the role of various enzymes in genetic manipulation.

c. Make use of the techniques involved in isolation, purification and separation of nucleic acids.

d. Apply different phylogeny techniques to find the ralation between dinstics living organism.

e. Appraise the use of genetic engineering principles for gene therapies.

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Watson, Molecular Biology of theGene.

B. Harvey F. Lodish, Molecular Cell Biology, 4thEdition.

C. Benjamin Lewin, GeneVII.

D. Benjamin Lewin,Cells.

WEB LINKS:

A. http://www.chem4kids.com/files/bio_nucleicacids.html

B. http://www2.chemistry.msu.edu/faculty/reusch/virttxtjml/nucacids.htm.

C. http://biology.about.com/od/molecularbiology/a/nucleicacids.htm.

D. http://chemed.chem.purdue.edu/genchem/topicreview/bp/1biochem/nucleic8html

MOLECULAR GENETICS (P)

1. PCR amplification ofDNA

2. Restriction enzyme digestion ofDNA

3. Ethanol precipitation of DNA

4. Agarose gel electrophoresis

5. Transformation of E. coli by electroporation

6. Preparative DNA Fragment Isolation from an AgaroseGel

7. Ligations of plasmid DNA to insertDNA

8. Transfection of mammalian cells usingLipofectamine

9. Cycle Sequencing Protocols For ABI3100

10. One Step Gene Assembly (GeneSynthesis)

IMMUNOLOGY

Course Learning Objectivess:

a. Specify the basic characterstics of the four major categories of microbes.

b. Identify the components of the immune system.

Course Detail:

UNIT

CONTENT

1

Overview of Immunology: Immune System, Functions of the Immune System; Types of

Immunity, Innate Immunity, Adaptive Immunity, Passive Immunity, Natural Immunity,

Acquired Immunity, Humoral vs. Cellular Immunity; Organs of the Immune System – Bone

Marrow; Cells of the immune system, T-Cells, B Cells, Dendritic Cells; Immune Response;

Measures of Immune Function.

2

Immune Response: Antigens, Chemical Nature of Antigens, Epitopes of an Antigen,

Recognizing and Antigen as Foreign; Antibodies, Basic Immunoglobulin Structure, Structure of

a Typical Antibody Molecule, Basic Immunoglobulin Function, Generation of Antibody

Diversity, Immunoglobulin Production; Factors Influencing Immunogenicity, Contribution of

the Immunogen, Contribution of the Biological System, Chemical Nature of Immunogens,

Types of Antigens; Super antigens, Determinants Recognized by the Innate Immune System;

Structure of an Antibody, Antibody Isotypes; Antigen-Antibody Interactions, Affinity and

Avidity,SpecificityandCrossReactivity;FactorsaffectingMeasurementofAntigen-antibody

Reactions, Agglutination Tests, Precipitation Tests; Tests for Cell Associated Antigens, Immuno

fluorescence, Flow Cytometry, Complement Fixation.

3

Immuno Chemistry: Humoral Immunity; Cell Mediated Immunity; Purification of Antigens,

Affinity Purification vs. Other Methods; Magnetic Particles, Antibody Purification, Antibody

Characterization, Pull-down Assays, Fusion Tag Protein Purification, Avidin-Biotin Systems,

Class Enrichment and Isolation, Containment Removal; Conjugation and Labelingof

Antibodies; Immunocolloidal Conjugates; Enzyme Linked Immunosorbent Assay, ELISA

Formats; Radioimmunoassay (RIA), The Technique, Separating Bound from Free Antigen.

4

Cell Response to Stress: Cell Death Machinery, Caspases as Death Effectors, Mitochondria

and Activation of Caspases, Death Receptors and Activation of Caspases, Inhibitors of Caspase-

Action:IAP Proteins, Ligation of Death Receptors and Cellular Stress-Induced Apoptosis,

Caspase-independent Apoptosis; Cellular Stress and Apoptosis, JNK Signaling and Cellular

Stress-Induced Apoptosis, Endoplasmic Reticulum and Cellular Stress-Induced Apoptosis, p53

and Cellular Stress-Induced Apoptosis, Ceramide and Cellular Stress-Induced Apoptosis;

Apoptosis;Cancer,CausesofCancer,WhataretheSymptomsofCancer?HowisCancer

Classified? How is Cancer Diagnosed and Staged?

5

Techniques in Autoimmunity: ELISA Technique, Applications, History, Types; Autoimmune

Disorders, Causes, Symptoms; Mechanism of HIV Infection, HIV Replication and

Transcription;DescriptionoftheHIVScreeningSimulation,StepsintheIndirectElisa,

Materials, Procedure; Radioimmunoassay, The Technique.

6

Serological Techniques: Types of Serological Tests, Complement Fixation Test (CFT),

Enzyme-Linked Immunosorbent Assay (ELISA), Agar Gel Immunodiffusion (AGID), Serum

Agglutination Test (SAT); Some Basic Tests – RA Factor; Blood Grouping, Rh Blood Types;

Coombs Test, Direct Coombs Test, Indirect Coombs Test, Coombs Reagent; New Serological

Techniques; Classification of Antigen-Antibody Interactions-Serological Tests;

Agglutination/Hemagglutination – Agglutination Tests; Passive Hemagglutination, Coomb’s

Test (Antiglobulin Test); Hemagglutination Inhibition, Precipitation Tests; Complement

FixationTest,Enzyme-LinkedImmunosorbentAssay(ELISA);WidalTest;VDRLTest;Cold

Agglutination Titer, Objectives, Principle, Materials, Procedure, Interpretation, Limitations of

the Procedure.

7

Advance Techniques in Autoimmunity: Gel Electrophoresis; Coomassie Brilliant Blue

Staining,WorkofAlkalinePhosphatase;Chromatography–BasicOperation;DifferentTypes

of Chromatography Methods, Paper Chromatography, Thin Layer Chromatography, Gas

Chromatography, FPLC; Optimizing Protein Purification; Different Modules and their

Operation.

Course Outcomes (COs):

Upon the completion of the course students will:

1. Understand the immunology and its two arms of immunity in detail.

2. Describe Information about humoral immunity, the involvement of B lymphocytes and its product,

antibody in immunity.

3. Another important topic of MHC that governs antigen processing will explained.

4. The ways through which T and B lymphocytes get activated so that they can play a role in the

elimination of antigens will be discussed.

5. Some of the diseases that involve the innate and acquired immunity will be taught along with

current vaccine strategies used.

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Stefan Dubel (edition), Handbook of TherapeuticAntibodies.

B. H. Zola, Monoclonal Antibodies.

C. F. Breitlingan d Stefan Dubel, RecombinantAntibodies.

D. Monoclonal Antibody Index: Cancer Diagnosis and Therapy (Volume1)

E. Monoclonal Antibody Index: Transplant, Infection, Heart (Volume2)

WEB LINKS:

A. http://www.biomed.drexel.edu/new04/content/academics/CourseMaterials/BMES212_2009W

INTER/ImmuneResponse.pdf

B. http://www.uta.edu/biology/britton/classnotes/1442/CH43.pdf.

C. http://www.nature.com/jid/journal/v133/n9full/jid2013287a.html

D. http://wwwlabdserotec.com/an-introduction-to-elisa.html.

IMMUNOLOGY (P)

1. Isolation and structure of immunoglobulins,

2. Monoclonal antibodies: production, purification and enzymaticfragmentation

3. To Produce Polyclonal Antibodies

4. ELISA (Enzyme Linked ImmunosorbentAssay)

5. Dot- ELISA (Enzyme Linked Immunosorbent Assay)

6. Radial Immuno Diffusion Test(RID)

7. Inheritance: Consequences of Clonal SelectionImmunofluorescence

8. Detection of a Single Antibody Producing Cell (Jerne PlaqueAssay)

9. MHC Polymorphism: HLA Typing byPCR

10. Phagocytosis

INTERMEDIARY METABOLISM

Course Learning Objectives:

a. Discuss the elementary biochemistry of the molecules of life and describe the relationship between

the structure and function of biomolecules.

b. To compare the structure and function of cells from different domains.

c. Discuss the development of cells and the role of cell specialization in multicellular organisms.

Course Details:

UNIT

CONTENT

1

Energy Metabolism: Laws of Thermodynamics, First Law of Thermodynamics, Second Law

of Thermodynamics, Exergonic and Endergonic Reactions, Standard free Energy change,

Calculation of Calorific Value of Foods; Energy Balance; energy control in Human Metabolism;

Energy Measurement; Measurement of Human Energy Expenditure; Respiratory Quotient

(RO); Factors contributing to the Total Energy Requirement, Basal Metabolic Rate;

Malnutrition, causes of Malnutrition, implications of Malnutrition impact of Malnutrition on

National Development, Prevention of Malnutrition

2

Digestion and Absorption of Carbohydrates: Digestion and Absorption of Carbohydrates,

Digestion, Absorption of Carbohydrates; Carbohydrate Metabolism; glycogen Metabolism;

Breakdown of Glycogen; Glycogen synthesis, Regulation of Glycogen Metabolism, Regulation

of Glycogen Synthesis by Covalent Modification, Hormonal Regulation of Glycogen Synthesis

and Breakdown; Glycolysis, Preparatory Phase of Glycolysis, Sequential steps involved in the

process of Glycolysis, Net reaction of Glycolysis; fates of Pyruvate Anaerobic Metabolism of

Glucose, Lactic Acid Fermentation, Alcoholic Fermentation, Regulation of Glycolysis;

Gluconeogenesis, Significance of Gluconeogenesis, Steps involved in Gluconeogenesis,

Aerobic Respiration; Oxidation of PYRUVATE INTO Acetyl CoA , structure of Pyruvate

Dehydrogenase Complex, Mechanism of Action of Pyruvate Dehydrogenase Complex,

Regulation of Pyruvate Dehydrogenesis complex; kreb’s Cycle or TCA cycle;Glyoxylate

cycle, Pentose Phosphate Pathway, substrate Level of Phosphorylation, Regulation of

Carbohydrate Metabolism, Metabolic Disorders due to Error in Carbohydrate Metabolism

3

Digestion and Absorption of Fats: Exogenouns and Endogenouns Lipids; Digestion and

Absorption of Fats, Hydrolysis of Lipids by different Lipases, Role of Bile Salt in Lipid

Absorption; Absorption of Lipids, Hormonal control of Transportation of Triacylgylcerols;

Glycerol Utilization; Fatty acid Activation, transportation of Fatty acyl CoA across the

Mitochondrial Membrane; Fatty Acid Oxidation, -Oxidation of Fatty Acids , Net reaction of

the -oxidation Pathway, oxidation of Odd chain fatty Acids, Oxidation of Unsaturated Fatty

Acids, Oxidation of Poly Unsaturated Fatty Acids, Regulation of Fatty Acid Oxidation, Fatty

Acid Oxidation in Peroxisomes, -Oxidation of Fatty Acids ; ketogenesis, Biosynthesis of Fatty

Acids, Formation of Malonyl-CoA; Long chain of fatty Acid Synthesis, Steps Involving during

Fatty Acids Synthesis, Overall Reaction, Synthesis of Long chain fatty Acids from Palmitate,

Fatty Acid Desaturation, Regulation of Fatty Acids Biosynthesis, Biosynthesis of

Triacylglycerols and Membrane Phospholipids; biosynthesis of Phosphatidic acid, Regulation of

Triacylglycerol Biosynthesis, metabolic Disorder due to Error in FatMetabolism

4

Digestion and Absorption of Proteins: Protein turnover; protein Degradation, Digestion of

Proteins by Gastric Secretion, Digestion of Proteins by Pancreatic Enzymes, Digestion of

Oligopeptide by enzymes of the Small Intestine; Amino Acid Metabolism; Metabolic Fates of

Amino Groups; Pathways of Amino Acid Degradation, Steps involved in the Catabolism of

Amino Acids; Transamination; Oxidative Deamination, Transport of Ammonia in The

Bloodstream by Glutamine; Glucose-Alanine cycle; Urea cycle; Enzymatic Reaction in

Mitochondrial Matrix, Enzymatic Reactions in Cytosol ; Regulation of Urea Cycle; catabolism

of Amino acids, Amino Acids that are Catabolized into Pyruvate; Metabolic Disorders due to

Error in Protein Metabolism

5

Biosynthesis & Degradation of Purines and Pyrimidines: De Novo Purine Nucleotide

Synthesis, Steps involved in De Novo synthesis of Purine Nucleotides; Regulation of Nucleotide

Synthesis; De Novo Synthesis of Pyrimidine Nucleotides; Biosynthesis of Thymine

(Deoxyribonucleotide) from Uracil (Ribonucleotide); Regulation of Pyrimidine Nucleotide

Biosynthesis, Synthesis of Nucleoside Triphosphates from Nucleoside Monophosphate;

Biosynthesis of Deoxyribonucleotides from Ribonucleotides; Salvage Pathway of Purines and

Pyrimidine Biosynthesis; degradation of Purines, Steps involved in the Formation of Uric Acid;

Degradation of Pyrimidine, Metabolic Defect of Nucleotide Metabolism; Vitamins, Fat-Soluble

Vitamin include A,D,E and K, Water-soluble vitamins are C, B1, B2, B6, B12,Niacin, Biotin

and Folic Acid, Absorption of vitamins; Minerals, Major Minerals, Trace Elements, Minerals

Metabolism

6

Regulation and Control Of Metabolism: Metabolic Control Analysis, Technique for

Analysing Metabolic Systems, Perturbation Analysis, Medical Applications; metabolic

pathways, Metabolic Fuels, Cell Metabolism is an economical Tightly Regulated Process,

MetabolicPathwaysareregulatedatthreeLevels;regulationofMetabolicPathways,Allosteric

Control of Metabolic Pathways, Respiratory control, substrate Availability, Hormonal

Regulation of Metabolic Pathways, flow of Key Metabolic substrates between different

Pathways; Cell Signaling, Intercellular Signaling, Intracellular Signaling

Course Learning Outcomes (COs):

Understand what is intermediary metabolism.

Become familiar with the concept of metabolic maps.

Differentiate between anabolism and catabolism.

Describe terms like glycolysis, gluconeogenesis &glyoxylate cycle.

Explain why metabolic pathways are not considered as closed systems.

Discuss the ways in which carbohydrate metabolic pathways, glycolysis and the citric acid cycle

interrelate with protein and lipid metabolic pathways.

Understand the linked metabolic pathways of fatty acid synthesis and protein synthesis with

carbohydrates and their derived substrates.

Appreciate the existence of common metabolic pools in cells.

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Hiram F. Gilbert, Basic Comcept in Biochemistry: A Student SurvivalGuide

B. Reginald Garret, Charles M. Grisham,Biochemistry

C. Voet&Voet, Text Book of Biochemistry: 3rd

Edition

D. Lehninger Principles of Biochemistry 4thEdition.

WEB LINKS:

A. http://www.wisegeek.com/what-is-energy-metabolism.htm

B. http://www.chem4kids.com/files/bio_methbolism.html

C. http://www.rsc.org/Education/Teachers/Resources/cfb/metabolism.htm

D. http://www.ds9a/metabolism/

INTERMEDIARY METABOLISM (P)

1. Amylase production test (demonstration of starchhydrolysis)

2. Cellulose production test (degradation ofcellulose)

3. Production of Pectolytic enzymes (degradation ofpectin)

4. Hydrolysis of gelatin, a protein (production ofgelatinase)

5. Caseinhydrolysis

6. Ureasetest

7. Hydrogen sulfide productiontest

8. Carbohydrate catabolism bymicroorganisms

9. Fermentation ofcarbohydrate

10. Microbial reaction in litmusmilk

MEMBRANE BIOLOGY

Course Learning Objectives:

a. Learning outcomes are what we might expect students to be able to do once they have mastered

these questions.

b. Instructors as to what activities students could take part in as a way to reach the learning outcomes

related to a central question.

Course Detail:

UNIT

CONTENT

1

Composition Of Biomembranes: Lipid Composition Of Biomembranes; Phospholipids

Glycolipids; Proteins, Integral Membrane Protein; Peripheral Membrane Proteins; Lipid

Anchored Protein; Carbohydrate Composition Of Biomembranes; Hydropathy Plots And

Membrane Topology; Membrane Topology; Composition Variation Between Membranes;

Difference Between Subcellular and Neuronal Membranes.

2

Model Membrane System: Monolayer, Planar Bilayer, Liposomes; Methods Of Liposome

Preparation , Isolation And Purification Of Membrane And Membrane Proteins, Detergents;

Uses Of Detergents, Density Gradient Centrifugation, Criteria Of Membrane Purification,

Enzyme Markers; Common Enzyme Markers

3 Membrane Structures: Polymorphic Structures Of Amphiphilic Molecules; Micelles; Bilayers;

Thermodynamic Forces That Affect The Formation Of Amphiphilic Molecules, Temperature,

Energy And Entropy; Critical Packing Parameter

4

Asymmetry In Membranes: Lipid And Protein Lateral And Transverse Asymmetry; Lipid

Rafts; Caveolae; Tight Junctions; Role Of Membrane Skeleton In Maintaining Cell Structure

And Membrane Asymmetry; Gate and Fences Model; RBC Membrane as a Model.

5

Membrane Transport: Study Of Different Transport System, Types Of Cell Transport; Free

Energy Change; Electrochemical Potential; Membrane Potential; Nernst Equation; Kinetics

Regulators And Inhibitors; Simple Diffusion; Facilitated Diffusion

6

Active And Passive Transport: Passive Transport, Glucose Transporter, Anion Transporter;

Active Transport; ABC Family Of Transporters, MDR Atpase Family, Cystic Fibrosis

Transmembrane Regulators(CFTR); Transport Processes Driven By Light, Bacteriorhodopsin,

Light-Driven Chloride Transport In Halorhodopsin; Group Translocation Specialized

Membrane.

7 Pores: Porins In Gram Negative Bacterial Membranes, OmpFPorin, OmpCPorin, LamB; Pore

Forming Toxins; Colicins, A-Hemolysin, Anthrax Toxin Protective Antigen; Aquaporins

8 Ion Channels: Voltage-Gated Ion Channels; Ligand-Gated Ion Channel; Leaky Channels.

9 Membrane Selectivity: Types Of Membrane Selectivity; Electrolyte Selectivity, Non-

Electrolyte Selectivity; Creation Of Membrane Transport Protein

Course Outcomes (COs):

Upon The Successful Completion Of The Course, Students Will Able to

a) Understand The Biochemistry Of Phospholipids And How They Are Organized Into Membranes.

b) Describe The Function Of Each Of The Four Components Of A Cell Membrane.

c) Differentiate Among Diffusion, Facilitated Transport, Facilitated Diffusion, Osmosis, And Active

Transport.

d) Describe The Six Classes Of Membrane Proteins And How Each Interacts With The Membrane.

e) Student will attain knowledge of cell biology and changes or losses in cell function.

f) Students will understand the cellular components and membrane transport.

g) Students can apply the knowledge of cell biology in research experiments.

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. William Stillwell, An Introduction to Biological Membranes from Bilayers to Rafts, 2013,

Elsevier.

B. Mary Luckey, 2008, Membrane StructuralBiology

C. P.S. Verma, Cell Biology, Genetics, Molecular Biology: Evolution and Ecology, S Chand & Co

Ltd, 2006

D. Albertset. Al., Molecular Biology of the Cell, 4th Edition, Garland Publisher,2002

WEB LINKS:

A. http://en.wikipedia.org/wiki/Biological_membrane

B. http://ncbi.nlm.nih.gov/books/NBK22361/

C. http://homepage.smc.edu/wissmann_paul/anatomy2textbook/phospholipids.html

D. http://themedicalbiochemistrypage.org/membranes.php.

GUIDELINES FOR SEMINAR

1. The seminar will be conducted in B.Sc. Second Year and will be of 100Marks

2. Students have to select a topic of their interest relevant to Advance Science or any areas of

interdisciplinary approach in the biologicalsciences

3. The seminar should cover the relevant information on current scenario of last 3years

4. There will be an internal evaluation by internal evaluating committee of the relevantdepartment

5. Evaluation will be done on the basisof

a) Relevance of topicselected

b) Way of presentation (language, ppt format, confidence, eye contact, body language and

other qualities ofpresentation)

c) Response toqueries

6. The committee will submit the marks to theuniversity.

7. An external evaluation will also be done at the end of term and the evaluation pattern will

remain same as that ofinternal.

YEAR III

ENVIRONMENTAL SCIENCE AND ECOLOGY

Course Learning Objectives:

a. This course aims at understanding the students in aspects of environmental problems,.

b. Solutions for these problems as well as environmental ethics which they should adopt to

attain sustainable development.

Course Detail:

UNIT

CONTENT

1

Renewable and Non renewable Resources: Renewable Energy, Agricultural Products,

Biomass, Water, Fossil Fuel, Radioactive Fuel; Renewable Resources; Economic Models; Non

renewable Energy, Humans Depend on Plants and Animals for Food, Nutrients as Food for

Plants, Mode of Intake of thirteen Essential Nutrients by the Plants; Manures and Fertilizers,

Manures, Types of Manures, Fertilizers, Bio fertilizers, Water; Fuel; Petroleum, Importance of

Petroleum, Levels and Flows Limits and Alternatives, Environmental Effects; Fiber, Textile

Fiber, Natural Fiver, Manmade Fiber Mineral Fiber, Polymer Fiber, Polyurethane Fiber;

Microfiber.

2

Conventional Fuel: Wind Energy; Solar Energy; Geothermal Energy; Biomass; Air Pollution;

Green house Gases; Implications for Agriculture and Forestry; Hydropower, Historical

Development; Firewood, Energy content, Heat Output, Measurement of Firewood, Combustion

by products, Combustion by product effects on Human health, Environmental Impact,

Environmental Concerns; Hilt’s Law, Early Uses as Fuel; Coal as Fuel, Coking Coal and Use of

Coke, Gasification, Liquefaction; Refined Coal, Industrial Processes, Cultural Usage;

Petroleum, EtymologyComposition.

3

Modern Fuel: Liquid Fuels for Transportation; First Generation Biofuels, Bioalcohols,

Biodiesel, Vegetable Oil, Bioethers, Biogas, Syngas, Solid Biofuels; Second Generation

Biofuels; Biofuels by Region, Issues with Biofuel Production and Use; Greenhouse Gase

Emissions, Factors Affecting Biogas Production, Design of Digester and Distribution of

Anaerobic Microorganisms, Effect of Metals on Biogas Production, Ammonia on Methanogens

andMethanogenesis, Alternate Feedstock, Other Wastes, Use of Spent Slurry, Advantages of

Biodiesel; Biodiesel Scenario in India, Biodiesel Experiments.

4

Microbes in Food Production: Fibers Produced by Bacteria, Bacterial Cellulose, Bacterial

Polyester, Applications of Bacterial Polyester; Developments in Wool, Biological Wool

Shearing; Developments in Silk, Ready Colored Yarns from Silkworm, Shape memory Silk

Yarn, Bio cosmetics from Silk Protein; Deodorant Fibers, Chitin, Chitosan; Alginate Fibers,

Collagen, Food Safety, Fermentation, Probiotics; Microbial Biopolymers, Xanthan, Alginate,

Cellulose, Poly Y glutamic acid, Levan, Exopolysaccharides; Foodborne Pathogens, Enteric

Viruses, Protozoan Parasites; Mycotoxins; Food Authenticity.

5

Bio fertilizer: Different Types of Bio fertilizers, Rhizobium, Azotobacter, Axospirillum,

Cyanobacteria, Azolla, Phosphate Solubilizing Microorganisms, AM Fungi, Silicate

Solubilizing Bacteria, Plant Growth Promoting Rhizobacteria, Liquid Bio fertilizers;

Characteristics of Different Liquid Bio fertilizers, Rhizobium, Physical Features of Liquid

Rhizobium, Axosirllium, Azotobacter, Acetobacter; Mass Production of Bacterial Biofertilizer,

Culturing of Microorganisms, Inoculums Preparation; Mass Production of MycorrhizalBio

fertilizer; Mass Production and Field Application of cyanobacteria, Multiplication in Trays,

Multiplication under Field Condition, Method of Inoculation of BGA in Rice Field; Mass

Production and Field Application of Azolla, Mass Multiplication of Azolla under Field

Conditions; Applications of Bio fertilizers, Seed Treatment, Seedling Root Dip, Main Field

Application; Azolla- The Best Feed for Cattle and Poultry, Inputs Required, Process Overview,

Activated Sludge, Surface aerated Basins, Constructed Wetlands, Filter Beds, Soil

Biotechnology, Biological Aerate3d Filters, Rotating Biological Contactors, Membrane

Bioreactors, Secondary Sedimentation, Tertiary Treatment, Filtration, Lagooning, Nutrient

Removal Nitrogen Removal, Phosphorus Removal, Disinfection, Odour Control, Package Plants

and Batch reactors, Sludge Treatment and Disposal, Anaerobic Digestion, Aerobic Digestion,

Composting, Incineration, Sludge Disposal, Treatment in the Recxeiving Environment, Sewage

Treatment in Developing Countries; H2 Production, Biophotolysis of Water by Microalagae and

Cyanobacteria, Hydrogenase dependent Hydrogen Production, Nitrogenase dependent

Hydrogen Production; Bio fertilizers and Bio pesticides; Solid Wastes, Sources of Solid Waste,

Management of Solid Waste; Management of Biomedical Wastes, Worm culture, Methane

Production; Single Cell Protein; Global Environmental Problems; Global Warming, Howto

Combat Global Warming, Green house Effect and Acid Rain, Greenhouse Gases; Ozone

Depletion, Impact of Ultraviolet Light, Issue, Ozone Depleting Substances, Ozone Hole.

6

Ecology: History of Ecology; Ecosystem, Understanding Ecosystems, Ecosystem Degradation,

Resource Utilization, components of Ecosystem; Energy Flow, Water Cycle, Carbon Cycle,

Oxygen Cycle, Nitrogen Cycle, Energy Cycle, Integration of Cycle in Nature; Food Chains and

Food Webs, Food Chains, Food Webs; Environment and Its Components, Natural Environment,

Manmade Environment.

7

Environment Pollution: Air pollution, Types of Air Pollutants, Global Warming and

Greenhouse Effect, Acid Rain, Prevention and Control of Air Pollution; Water Pollution,

Sources of Water Pollution, Ground Water Pollution, Eutrophication, Methods for Control of

Water Pollution and Water Recycling; Noise Pollution, Sources of Noise Pollution, Effects of

Noise Pollution, Prevention and Control of Noise Pollution; Solid Waste Pollution, Control of

Solid Waste Pollution.

8

Global Environmental Issues: Environmental Degradation, Climate change, Ozone Layer

Depletion, Global Warming, Loss of Biodiversity, Land Degradation, Soil Degradation; Other

Environmental Issues, Conservation of Species, Energy Crisis, Nuclear Issues, Overpopulation,

Waste Management; Environmental Health; Genetic Engineering Risks and Impacts, GE Health

Risks, GE Environmental Impacts; Nanotechnology; Intensive Farming.

Course Outcomes (COs):

Upon the successful completion of the course, students will able to

a) Define important scientific/ecological terms.

b) Describe important ecological processes

c) Use the scientific method to design an ecological study in the lab and/or field.

d) Demonstrate knowledge of the important ecological principles operating at different levels of

organization"

LEARNING SOURCE: Self Learning Materials

ADDITIONALREADINGS:

A. Ackerman, F., 2000, Waste Management and Climate Change, Local Environment, 5(2), pp.

223- 229

B. Austrian Federal Government, 2001, Third National Climate Report of the Austrian Federal

Government, Vienna,Austria.

C. Gerben J Zylstraa and Jerome J Kukor, What is environmental biotechnology? Current Opinion

in Biotechnology 16(3):243-245,2005

D. Chanton, J. and K. Liptay, 2000, Seasonal variations in methane oxidation in a landfill cover

soil as determined by an in situ stable isotope technique, Global Biogeochemical Cycles,

14,pp.51-60

WEB LINKS:

A. http://www.eschooltodya.com/energy/non-renewable-energy/what-is-non-renawable-energy.html

B. http://www.conserve-energy-future.com/

C. http://ecosystems.psu.edu/youth/sftrc/environ-series/rnr-mat.

D. http://en.wikipedia.org/wiki/Environmental_science

INDUSTRIAL BIOCHEMISTRY

Course Learning Objectives:

a. Describe the main steps and processes used to products in industry.

b. Discover new useful microorganisms and store them reliably.

c. Understand ethical and commercial issues such as record keeping .

Course Detail:

UNIT

CONTENT

1

Introduction to Fermentation Technology: Isolation and Screening of Industrially Important

Microbes, Various Methods of Achieving Isolation, Various Methods of Achieving Isolation;

Inoculums Preparation; Strain Improvement; Primary and Secondary Detection of

Microorganisms, Primary Screening, Secondary Screening, Secondary Screening; Biological

Assay of Fermentation Products, Limitations of Bioassay, Diffusion Assay, Turbid metric

Assay, Metabolic Response Assay, Enzymatic Assay; Advantages of Bioprocess OverChemical

Process

2

Fermentation Process: Batch Culture, List of Reagents and Instruments, Procedures; Fed-batch

Fermentation, Fixed Volume Fed-batch, Variable Volume Fed-batch, Advantages and

Disadvantages of Fed-batch Reactors, Equipment; Control Techniques for Fed-batch

Fermentation; Modeling Fed-batch Fermentations, Fixed volume Fed-batch, Variable Volume

Fed-batch, Models of Possible Situations that may Occur in a Fed-batch Fermentation;

Parameters used to Control Fed-batch Fermentations, Calorimetry, Specific Growth Rate,

General Feeding Mode, Proton Production; Fluorescence, Parameters to Start and Finish the

Feed and Stop the Fed-batch Fermentation, Preliminary Knowledge Required to Implement

Fed-batch, Eventual Inhibitions from the Substrate and/ or Product, Open-loop Performance,

Feed-back Control Algorithm; Some Examples of Fed-batch use in Industry

3

Fermentation Conditions: Fermenters; Microorganisms Used and Fermentation Process,

Importance and Uses; Process of Fermentation; Control and Monitoring Fermentation System,

Temperature, Gas Flow Rate, Liquid Flow Rate, Pressure measuring and Controlling Devices,

Agitation Measuring and Controlling Device; Foam Sensing, Dissolved Oxygen Monitoring, pH

Monitoring Devices, PID Control Systems

4

Types of Fermenters: Air-Lift Fermenter, Fluidized Bed Bioreactor; Packed Bed Bioreactor,

Continuous Culture; Fed Batch Culture, Fixed Volume Fed-batch, Variable Volume Fed-batch;

Advantages and Disadvantages of the Fed-batch Reactors, Continuous-Flow Stirred-tank

Reactor

5

Special Fermenters: Fuidized Bed Reactor (FBR),Basic Principles, History and Current Uses,

Advantages, Disadvantages; Current Research And Trends, Tubular Reactors, Gas Feed

Systems, Liquid Metering Pumps, Back Pressure Regulators, Cooling Condensers, Gas/Liquid

Separators, Control and Data Acquisition Systems

6 Computer Application in Fermenters: Computer Based Fermentation; Pre lab; Fermenter and

Sensors; Control System, Function; Methods, Sample Experiments and Discussion

7

Microbial Products: Microbial Enzyme- Amylase; Production of Amylase; Microbial

Enzyme- cellulose, Cellulose- Producing Microorganisms, Fermentation Production of

Cellulose; Microbial Enzyme- Pectinase, Microbial enzyme- Protease; Industrial Production of

Alcoholic Beverages, Alcoholic Beverages- wine, Alcoholic Beverages- Beer, Organic Acid;

Citric Acid, Production of citric Acid, Acetic Acid, Production of Acetic Acid; Gluconic Acid;

Lactic Acid, Production of Lactic Acid

8

Microbes and Environment: Microbes in Mineral Recovery; Bioleaching, Bioleaching

Mechanism, Advantages of Bioleaching, Disadvantages of Bioleaching; Biosorption, Biosorbent

Material, Biosorption Mechanisms; Microbial Recovery of Petroleum- Process,MEOR

Advantages, MEOR Disadvantages; Microbial Degradation Of Xenobiotics, Properties of

Xenobiotic Compounds, Hazards Post by Xenobiotic Compounds, Mechanism Involved in

Biodegradation of Xenobiotics; Sewage Biodegradation, Sewage Treatment;Biodegradation and

Bioremediation, Bioremediation; Productionof Biomass, Bioethanol Production; Production of

Single Cell Protein ; Mushrooms, Production of Edible Mushrooms, Process of Mushroom

Production

9

Production of Bacterial and Fungal Polysaccharides: Polyhydroxyalksnoates, Properties,

Microorganism that Synthesize PHAs; Industrial Scale Production of PHA; Application of

PHAs In industry; MICROBIAL Lipids, Potential Microorganism for the Production of Lipids,

Method for Lipid Production; Bioinsecticides, Example, Application, Advantages,

Disadvantages; Industrial Production of Penicillin, Industrial Production of Penicillin, Steps for

Production of Penicillin; Industrial Production of streptomycin, Mechanism ofAction;

Production of Vitamin B12, Synthesis and Industrial Production; Riboflavin, Industrial

synthesis

Course outcomes

1. Describe the main steps and processes used to produce biological products in industry.

2. Discover new useful microorganisms and store them reliably for later use.

3. Evaluate which molecular techniques are applicable to improve production(including transfer of

useful genes to microorganisms that are more amenable to large-scale production and the use of

molecular techniques to block and enhance specific metabolism).

4. Understand ethical and commercial issues such as record keeping, confidentiality, patenting, and

licensing.

5. Perform microbiological investigations, observe and evaluate the data obtained, and report the

findings accurately and precisely

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Pelczar MJ, Chan ECS, Kleig NR, 1993, Microbiology, Tata McGrawHill.

B. Tom Betsy, & Jim Keogh, 2005, Microbiology Demystified, McGrawHill.

C. R C Tilton, 2002, Microbiology, 10thed, McGrawHill.

D. Stuart Hoggy, 2005, Essential Microbiology,Wiley.

WEB LINKS:

A. http://www.water.me.vccs.edu/courses/env108/Lesson3_print.htm

B. http://www.google.co.in/?gws_rd=cr&ei=Nx9uUrn0GMA4rgeB44CgCA#q=isolation+of+microo

rganisms

C. http://www.google.co.in/?gws_rd=cr&ei=Nx9uUrn0GMA4rgeB44CgCA#q=fermentation

D. http://en.wikipedia.org/wiki/Biochemist

INDUSTRIAL BIOCHEMISTRY (P)

1. Determination of aluminum, iron, and zinc in plants by nitric and perchloric acid digestion and

analysis by ICP-OES

2. Determination of soluble protein content by Lowrymethod

3. Polyacrylamide gel electrophoresis (PAGE) and isozymeanalysis

4. Determination of tryptophan content in maize flour by papainhydrolysis

5. Estimation of total amylase [(α-amylase (EC 3.2.1.1) and β-amylase (3.2.1.2)]activity

6. Extraction and estimation of total lipid content inoilseed

7. Estimation of total solublesolids

8. Estimation of structuralcarbohydrates

9. Estimation of sucrose synthaseactivity

10. Estimation of nitrogenaseactivity

NUTRITIONAL BIOCHEMISTRY

Course Learning Objectives:

a. Scope of the course Life is a biochemical process involving thousands of reactions occurring in an

organized manner.

b. These reactions are collectively called metabolism.

c. The major objective of learning this course is the complete understanding of all the metabolic

reactions at a molecular level

d. This course is related to almost all the life sciences and without a background knowledge of

this course, a thorough understanding of health and well-being is not possible

Course Detail:

UNIT

CONTENT

1

Introduction to Nutritional Biochemistry: Energy Content of the Food; Measurement of

Energy Expenditure; Respiratory Quotie3nts of Food Stuffs; Specific Dynamic Action; BMR,

Measurement of BMR and Factors Influencing BMR; Daily Energy Requirement; Importance of

Energy for Various Activities; Calorific Equivalent of Major Nutrients.

2

Dietary Requirements: Recommended Dietary Allowances for Infants and Children;

Recommended Dietary Allowances for Children, Adolescent; Recommended Dietary

Allowances for Pregnant and Lactating Women; Role of Dietary Fat, Healthier Dietary Fat,

Harmful Dietary Fat; Role of Dietary Fiber; Antioxidants, Antioxidant Process, Types of

Antioxidants; Proteins, Protein Content of Diets of People in different Parts of India.

3

Amino Acids and Proteins: Essential Amino Acids; Biological Value of Proteins; Nitrogen

Balance; Protein Content of Diets of People in Different Parts of India; Protein Calorific

Malnutrition.

4

Minerals: Dietary Macro Minerals, Macro Mineral: Calcium, Macro Mineral: Phosphorus,

Macro Mineral Magnesium, Macro Mineral Sulphur, macro Mineral Potassium, Macro Mineral

Sodium; Trace Minerals, Trace mineral Iron, Trace mineral Iodine, Trace Mineral Zinc, Trace

Mineral Copper; Disorder caused by Deficiencies of Minerals, Iron, Iodine, Zinc Calcium,

Fluoride, Sodium, Potassium.

5

Nutrition and Body Defenses: Effects of Drugs on Food and Nutrients; Impact of Drugs on

Food and Nutrition; Side Effects of Drugs and Other Medications, Drug Nutrient Interaction

Nutritional Therapy, Food Preparation and Management; Role of Diet and Nutrition in the

Prevention and Treatment of Disease, Beat Hear Disease.

6

Growth and Development from Infancy to Adulthood: Somatic, Physical Brain and Mental

Development, Puberty, Menarche, Prepubertal and Pubertal Changes, somatic and Physical

Changes, Brain and Mental Development, Puberty, Menarche, Pre pubertal and Pubertal

Changes; Factors Affecting Growth and Development; Impoutance of Nutrition for Ensuring

Adequate Development; Growth Monitoring and Promotion- Use of Growth Charts and

Standards; Preventions of Growth Faltering.

7

Nutrition during Pregnancy: Non nutritional factors Affecting Pregnancy Outcome, Physical

Factors, Dietary Choices; Importance of Adequate Weight Gain during Pregnancy, Calorie

Requirements and Weight; Antenatal Care and its Schedule; Nutritional Requirements during

Pregnancy; Modifications of Existing Diet and Supplementation; Deficiency of Nutrition;

Common Problems of Pregnancy and their Managements; Adolescent Pregnancy.

8

Nutrition during Lactation: Nutritional Requirements during Lactation; Dietary Management

during Lactation; Food Supplements Required during Lactation; Galactogogues; Preparation for

Lactation; Care and Preparation of Nipples during Breastfeeding.

9

Nutrition during Infancy: Physiology Relevant to Feeding and Care; Colostrums- Its

Composition and Importance in Feeding; Initiations of Breast feeding; Advantages of

Breastfeeding; Basic Principles of Breastfeeding; Supplementary Foods; Initiation and

Management of Weaning; Baby led Weaning; Bottle Feeding Circumstances under which bottle

feeding; Care and Sterilization of Bottles; Preparation of Formula; Mixed Feeding;

Breastfeeding ad Artificial Feeding.

10

Geriatric Nutrition: Nutrition Meeting the Needs of Elderly; Age Related Changes and

Nutrition, Physical Changes, Perceptual Changes, Gastrointestinal Changes, Reduced

Metabolism, Less Saliva and Dentition problems; Changes in Nutritional Needs; Assessment of

Nutritional Status, Choosing a Dietary Approach to Nutritional Status Assessment, Common

Methods for Dietary Data Collection, Disease State Considerations, Nitrogen Balance Studies,

Monitoring Response, Other Laboratory Indices; Parameters of Assessment, Elements of the

Assessment.

Course Outcomes (COs): Upon the successful completion of the course, students will able to

a) Provide basic understanding of carbohydrates, lipids, and proteins and their roles in normal

biological processes.

b) discuss the role of selected nutrients on key metabolic pathways in the human body

c) Intellectual rigour Knowledge of a discipline identify the integrated role of dietary carbohydrate,

pre- and probiotics, essential amino acids, essential fatty acids and micronutrients in maintaining

human health

d) Intellectual rigour knowledge of a discipline evaluate the therapeutic role (including actions,

interactions, contraindications, cautions and toxicity) of key micronutrients in maintaining and

regaining health

e) Intellectual rigour Knowledge of a discipline apply and interpret analytical methods appropriate to

the analysis of selected nutrients in food.

f) Understanding of food therapy

g) Health and well being through biochemical pathway functions.

h) Role of nutrients in biochemical pathways in the body.

i) Explaintion of the the biochemical absorption, storage and metabolic function of macro

and micronutrients.

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Tom Brody, Nutritional Biochemistry, 2nd

Edition, AcademicPress

B. Maria C. Linder, Elsevier; Nutritional biochemistry and metabolism: With clinical applications,

2nd

Edition.

C. Annual Editions: Nutrition 11/12, McGraw-Hill/Dushkin; 23Editions.

D. Bliss M, the Discovery of Insulin. Chicago, University of Chicago Press, 1982, p155.

WEB LINKS:

A. http://www.acefitness.org/cettifiednewsarticle/2882/resting-metabolic-rate-best-ways-to-

measure-it-and/

B. http://www.fao.org/docrep/007/y5686e04.htm

C. http://mccuescience.com/uploads/SDAreview.pdf.

D. http://en.wikibooks.org/wiki/Fundamentals_of_Nutrition/Nutritional_Biochemistry

CLINICAL BIOCHEMISTRY

Course Learning Objectives:

a. Clinical Biochemistry mainly deals with the biochemical aspects that are involved in several clinical

conditions.

b. The results of qualitative and quantitative analysis of body fluids assist the clinicians in the

diagnosis, treatment, prevention of disease, drug monitoring, forensic investigation, tissue and

organ transplantation.

Course Detail:

UNIT

CONTENT

1

Introduction to Clinical Biochemistry: Introduction to Clinical Biochemistry, Importance of

Clinical Biochemistry; Introduction to Clinical Pathology, Tools of Clinical Pathology,

Importance of Clinical Pathology; Applications of Clinical Biochemistry.

2

Glucose: Metabolism and Disorder: Glycolysis-An Overall Equation; Anaerobic and

Aerobic Glycolysis, Anaerobic Glycolysis Pathway, Aerobic Glycolysis Pathway;

Glycogenesis; Regulation of Blood Glucose; Diabetes Mellitus, Causes of Diabetes,Symptoms

of Diabetes, Diagnosis of Diabetes; Glucose Tolerance Test, Evaluation the Results of the Oral

Glucose Tolerance Test, Preparation of Test.

3

Lipids: Metabolism and Disorder: Structure of Fatty Acids; Phospholipids; Steroids;

Nomenclature and Terminology; Essential Fatty Acids, Food Sources, Human Health; Omega

3 fatty acids; Uses; Attention Deficit Disorder; Dietary Sources, Available Forms; Insulin,

Uses in the Heart and Brain, Production; Acetyl CoA; Ketosis andKetoacidosis.

4

Structure, Function and Classification of Protein: Classification of Protein by their

functions, by location in living Cell and by Post translational Modification; Structure of

Protein; Peptide Bond, Properties of Amino Acids; Protein Structure Determination, Secondary

Structure, Super secondary Structure, Tertiary Structure, Quaternary Structure; Non covalent

Forces; Covelent Forces; Protein Denaturation; Protein-Protein Interactions; Gelation,

Quantitative Determination of Creatinine in Human Serum, Quantitative Determinationof

Total Protein in Human Serum.

5

Enzymology: Enzyme Kinetics; Alterations in Enzyme Activity; Regulation of Enzyme

Activity; Factors Affecting Enzyme Activity, Enzyme Concentration, Substrate Concentration,

Effects of Inhibitors on Enzyme Activity, Temperature Effect s, Effects of pH; Mechanism of

Enzyme Action, Lock and Key Theory, Induced Fit Theory, Nature of Active Site and

SubstrateInteraction;DiagnosticSerumEnzymes,Aldolase,CreatinePhosphokinase,Gamma

GlutamylTranspeptidase, Lactic Dehydrogenase, Lipase, Transaminases.

6

Minerals and Vitamins: Minerals; Sulphur; Boron; Iodine;

Methylsulphonylmethane(MSM); Vitamins; Types of Vitamins; Need of vitamins; Vitamin A:

Retinol and Carotene; Vitamin B1 : Thiamine; Vitamin B2: Riboflavin; Vitamin B3: Niacin;

Vitamin B5 : Pantothenic Acid; vitamin B6: Pyridoxine and Pyridoxal Phosphate; Vitamin

B9:Folic Acid)Folate and PteroyiglutamicAcis) Folacin; Vitamin B12: Cyanocobalamin;

Vitamin C: Ascorbic Acid; Vitamin D: Cholecalciferol and Sunshine Vitamin; Vitamin E:

Alpha-tocopherol;VitaminH:Biotin;VitaminK:Phytonadione;VitaminP:Bioflavonoidsand

Phytochemicals; Vitamin Deficiency Diseases; Types of Vitamin Deficiencies

7 Blood and Urine Composition: Blood, Composition of Blood, Ageing Changes in the Blood;

Urine, Physical Characteristics, Composition of Urine.

8

Liver Functions: Uses of Liver Function Tests, Limitations; Classification of Liver Function

Tests; Serum Bilirubin, Types of Bilirubin, Diagnostic Value of Bilirubin Levels, Prognostic

Value of Bilirubin Levels; Urine Bilirubin; Urobilinogen; Enzymes that Detect Hepatocellular

Necrosis Aminotransferases, Mild, Moderate and Severe Elevations of Aminotransferases;

AST; ALT Ratio; Enzymes that Detect Cholestasis, Alkaline Phosphatase, Y

GlutamylTranspeptidase, Other Enzymes that Detect Cholestasis; Tests of the Liver’s

Biosynthetic

Capacity, Serum Proteins, Albumin, Prealbumin, Serum Ceruloplasmin, Procollagen III

Peptide.

9

Kidney Functions: Anatomy of Kidney, Structure, Blood Supply, Nephron; Renal Physiology,

Excretion of Wastes, Filtration, Reasorption and Secretion, Water Homeostasis, Electrolyte

Homeostasis, Blood Pressure Homeostasis, Hormones.

Course Outcomes (COs):

Upon the successful completion of the course, students will able to

a) Explain the biochemical mechanisms and path physiological processes responsible for common

biochemical disorders

b) Explain the rationale and theoretical basis for methods used in the diagnosis of common

biochemical disorders

c) Compare and contrast the different patterns of biochemistry test results observed in various disease

states

d) Demonstrate competency in performing common analytical techniques used in clinical chemistry

e) Understanding of analytical instruments in use in the routine clinical laboratory

f) Discuss the biochemistry and pathophysiology associated with tests performed in a clinical

biochemistry laboratory

g) Identify and interpret common result patterns related to pathophysiology in relation to routine clinical

biochemistry

LEARNING SOURCE: Self Learning Materials

ADDITIONAL READINGS:

A. Nessar Ahmed, Clinical Biochemistry, OUP Oxford, 2010, Jaypee Brothers

B. VP Acharya, PK ohanty, A Complete Work bood on Clinical Biochemistry, 2010JPH

C. N Haridas, Biochemistry Made Easy: A Problem-Based Approach, 2012, Jaypee Brothers

D. Takkella Nagamma, MCQs in Biochemistry with Explanation,2013

WEB LINKS:

A. http://www.faculty.ksu.edu.sa/52876

B. http://www.studymode.com/essays/Introduction-To-Biochemistry-1506934.html

C. http://www.allbookez.com/basic-biochemistry-lecture-notes

D. http://en.wikipedia.org/wiki/Clinical_chemistry

CLINICAL BIOCHEMISTRY (P)

1. To Determine the Blood group of and individual by Slide Agglutination Test.

2. Erythrocyte Sedimentation Rate(ESR)

3. Collection of Specimens for Analysis

4. Estimation of Serum Cholesterol

5. Estimation of Blood Sugar

6. Estimation of Serum Protein

7. Estimation of Serum Bilirubin

8. Estimation of Serum Uric Acid

9. Estimation of Serum Alkaline Phosphates Activity

10. To Estimate the Hemoglobin Content of Human Blood

PROJECT WORK/ INDUSTRIAL TRAINING

The topic of the project should be selected by the students themselves in consultation with the industry as

well as the faculty guide. The project work is to be submitted to the training coordinator by before the end

of final year examinations.

The project work (including the contact details of the project guide) is to be forwarded to the Training

Coordinator.

Candidate will come to college to get their project checked by their training coordinator.

Project Work: The synopsis should be, mention the project title, indicate the problem identification and

approach towards the project the following points

1. Brief profile of Industry

2. Purpose / Objectives of the Project /Research

3. Scope

4. Methodology

5. Need for study.

6. Organization’s benefit / gain as a result of the project

7. Name, Contact Address, Telephone no., Cell no., e-Mail ID of the project guide in the

organization in order to seek timely confidence reports about the project progress / conduct from

the training organization.

8. Lastly, following information is to be included in the end on a separate page for:

a. Guest Lectures

b. Event Sponsorships

c. Industrial Visits

d. Management Development Programs Faculty