macromolecules 3: proteins
DESCRIPTION
Macromolecules 3: Proteins. Fibrous (structural) proteins. Only have primary and secondary structures Water insoluble VERY tough, may also be supple or stretchy Parallel polypeptide chains in long sheets or fibres STRUCTURAL proteins – collagen, cartilage, tendons, blood vessel walls - PowerPoint PPT PresentationTRANSCRIPT
Macromolecules 3: Proteins
Fibrous (structural) proteinsOnly have primary and secondary structures
• Water insoluble• VERY tough, may also be
supple or stretchy• Parallel polypeptide chains
in long sheets or fibres• STRUCTURAL proteins –
collagen, cartilage, tendons, blood vessel walls
• CONTRACTILE proteins – actin and myosin
Globular proteinsHave all four levels of
protein structure• Water soluble• Tertiary structure critical
to function• CATALYTIC (enzymes)• REGULATORY –
hormones (insulin)• TRANSPORT
(haemoglobin)• PROTECTIVE
(immunoglobulins)
Proteins• > 50% of the dry mass of a cell is
proteinProteins are used for:• Structural support• Energy storage• Transport of other substances• Signalling from one part of the
organism to another• Movement• Defence against foreign substance• Enzymes• Humans have tens of thousands of
different proteins• Most structurally sophisticated
molecule, due to unique 3D shape or conformation
Types of protein1. Structural
support (Fibrous proteins)
Silk: cocoons and webs Keratin: hair, horns, skin, nails, wool, beaksCollagen: tendons and ligaments
2.Globular proteins (e.g.Enzymes)
Amylase CatalasePepsinTrypsinDNA helicaseDNA synthaseEtc etc etc…
Globular proteins: Hormones
• Insulin• ACTH• Vasopressin• Somatostatin• Prolactin• Growth hormone
Globular proteins:Transport proteins
Haemoglobin, myoglobin: transport of essential substances (oxygen, carbon dioxide)Myoglobin was the first protein to be thoroughly described
Globular proteins: Energy storage
Ovalbumin, Casein (milk protein), storage proteins in plant seeds
Movement proteinsActin and myosin form muscle fibresAnimation of actin/myosin
Receptor proteins (also pumps, channel proteins)
• Adrenergic receptors
• G-protein receptors• Cannabinoid
receptors• Opioid receptors• Aquaporin
channels• Na/potassium
pump proteins
8. Immune function:Antibodies (Immunoglobulins)
Globular soluble proteins: IgG, gA, IgM,
Amino Acid (Monomers)Amino acid structure:
NH3 - C - COOH
Amino acids differ due to the R (functional) group
The structure of the R-group determines the chemical properties of the amino acid
Proteins Chemical composition C-H-O-N-(S) Proteins are made up of smaller monomers called AMINO
ACIDS Amino Acids differ ONLY in the type of R (functional)
group they carryAmino acids composed of 3 parts1. Amino Group2. Carboxylic group3. Functional ®-group (Makes 20 different amino acids)
20 Amino Acids
Amino Acids link together to form polypeptides
• 2 Amino Acids form a covalent bond, called a PEPTIDE BOND,through a condensation reaction to form a dipeptide
• Multiple amino acids can bond to each other one at a time, forming a long chain called a POLYPEPTIDE
Peptide Bonds – link amino acids
Protein shape• Each protein has a
specific, and complex shape
• Proteins are composed of one or more polypeptides
• Different shapes allow proteins to perform different functions
Protein Shape Determines Function• Proteins with only primary and secondary structures are
called fibrous proteins (claws, beaks, keratin, wool, collagen, ligaments, reptile scales)
• Proteins with only 1,2,3 shapes are called globular proteins
• If a protein is incorrectly folded, it can’t function correctly
• Not understood how proteins fold themselves, seem to have molecules called chaperone proteins or chaperonins that assist others
• A protein is denatured when it loses its shape and therefore its ability to function correctly
2020
Four Levels of Protein Structure/ Conformation
1. Primary - unique linear sequence in which amino acids are joined, can have dire circumstances if changed (insulin)
2. Secondary - refers to three dimensional shapes that are the result of H bonding at regular intervals, due to interactions between the amino acid backbones• alpha helix is a coiled
shape• beta pleated sheet is
an accordion shape
3. Tertiary Complex 3-D globular
shape due to interactions between R groups of amino acids in it• Globular proteins such
as enzymes are held in position by these interactions
4. Quaternary Consist of more than one
polypeptide chain subunits, associated with interactions between these chains 2119
Primary Structure• A unique sequence of
amino acids in a long polypeptide chain
• Involves peptide bonds between the carboxyl and amine groups
• Any changes in primary structure will affect a protein’s conformation and its ability to function• Example: Sickle cell anemia
LYS VAL PHE GLY ARG CYS
Sickle cell anaemiaSickling occurs due to a mutation of the Hb gene, associated with replacement of glutamic acid by valine
Secondary StructureMade by hydrogen bonds between the backbone of the amino acids (amino
group and carboxyl groups)
• α-helices: area with a helical or spiral shape. Held together by H bonds between every 4th amino acid
• β-pleated sheets: area where 2 or more regions of the polypeptide chain lie in parallel
αhelix a β-pleated sheet
• The bonds involved are hydrogen bonds• Large proteins will have regions containing both
structures
Tertiary Structure: FOLDINGThe protein folds up since various
regions on the secondary structure are attracted to each other:
1. Disulfide Bridges: strong covalent bonds between cysteine’s sulfhydryl (-SH) groups
2. Ionic Bonds: between positively and negatively charged side chains
3. Hydrogen Bonds: between polar side groups
4. Hydrophobic Interactions: non-polar side chains end up on the inside of a protein, away from water
Quaternary StructureComplex proteins exist as
aggregations of 2 or more polypeptide subunits
QUATERNARY STRUCTUREE.g. immunoglobulins
• The bonds involved are the same as those for tertiary structure
Chain 1
Chain 3 Chain 2
Protein denaturationProtein denaturation refers to loss of 3 – dimensional structure (and usually also biological function) of a protein – die to changing of the bonds that maintain secondary and 3rd degree structure, even though the amino acid sequence remains unaltered
Denaturation can be caused by:• Strong acids and
alkalis – profound pH change
• Heavy metals – may disrupt ionic bonds
• Heat, radiation, UV radiation
• Detergents and solvents
Protein ConformationPrimary Structure – sequence of amino acids
Secondary structure – Folding and coiling due to H bond formation between carboxyl and amino groups of non-adjacent amino acid. R groups are NOT involved.
Tertiary structure – disulfide bridges, ionic bonding, or H-bonding of R-groups
Quaternary structure – 2+ amino acid chains R- group interactions, H bonds, ionic interactions
Primary Structure• A unique sequence of
amino acids in a long polypeptide chain
• Any changes in primary structure can affect a protein’s conformation and its ability to function• Example: Sickle cell anemia
Primary structure• The sequence of amino acids• Involves peptide bonds between the carboxyl and amine groups
LYS VAL PHE GLY ARG CYS
Sickle cell anaemia• Sickling
occurs due to a mutation of the Hb gene, associated with replacement of glutamic acid by valine
Secondary Structure• Segments of the
polypeptide strand repeatedly coil or fold in a pattern which contributes to the overall conformation
• Made by hydrogen bonds between the backbone of the amino acids (amino group and carboxyl groups)
Structures formed include:• α-helices: area with
a helical or spiral shape. Held together by H bonds between every 4th amino acid
• β-pleated sheets: area where 2 or more regions of the polypeptide chain lie in parallel
Secondary Structure
Secondary structure• The amino acids in the primary structure can bond
together to form :
• a) An alpha helix b) a beta pleat
• The bonds involved are hydrogen bonds• Large proteins will have regions containing both
structures
Tertiary StructureMade of irregular contortions from interactions between side chains (R groups)1. Hydrogen Bonds: between polar side groups2. Ionic Bonds: between positively and negatively charged side chains3. Hydrophobic Interactions: non-polar side
chains end up on the inside of a protein, away from water—caused by water excluding these side chains from H bond interactions. Once together, held in place by dipole-dipole interactions
4. Disulfide Bridges: strong covalent bonds between cytosine’s sulfhydryl (-SH) groups
TERTIaRY STRUCTURE• The protein molecule undergoes further
twisting and folding to form a 3 dimensional shape
• The structure is held in place by interactions between R-groups of the different amino acids
Tertiary Structure
Quaternary StructureThe overall protein structure that
results from the aggregation of 2 or more polypeptide subunits
QUATERNARY STRUCTURE• Proteins can contain more than one protein chain• E.g. immunoglobulins (form antibodies)
• The bonds involved are the same as those for tertiary structure
Chain 1
Chain 3 Chain 2
Review: The Four Levels of Protein Folding
Denaturing of ProteinProteins can be denatured by:• Transfer from aqueous solution to an organic
solvent (e.g. chloroform)
• Any chemical that disrupts H-bonds, ionic bonds, & disulfide bridges
• Excessive heat
• Changes in pH
Denaturation• Protein conformation depends on the physical and
chemical conditions of the protein’s environment• pH, salt concentration, temperature, and other aspects of
the environment (aqueous or organic solvent) can unravel or change the conformation of the protein.
• Change in protein shape causes it to lose its function• Some proteins can renature and reform their
conformation, other cannot.
TESTING FOR PROTEINS• Measure out 2cm3 of test solution
into a test tube• Add 2 cm3 of Biuret solution• Shake and record colour change for
each sample
• Positive result = colour change from blue to lilac