chemistry
DESCRIPTION
Chemistry. Macromolecules. Macromolecules. Small molecules linked together to create large molecules Have shape created by hydrogen bonding, sulfhydryl bonding, polarity, etc. FORM FITS FUNCTION Ex. Proteins do ‘everything’. Protein. Linus Pauling. Stanley Miller. - PowerPoint PPT PresentationTRANSCRIPT
Chemistry
Macromolecules
Macromolecules
• Small molecules linked together to create large molecules
– Have shape created by hydrogen bonding, sulfhydryl bonding, polarity, etc.
• FORM FITS FUNCTION
– Ex. Proteins do ‘everything’
Protein
Stanley Miller Linus Pauling
Carbon bonds 4 times in multiple ways
Creates great variety
Hydrocarbons
ISOMER
Isomers = molecules
with the same formula but
different structural
formulae; not isotope
AMP
ATP
GTP
Differences in functional groups
What is a functional group?
Ethane
Ethanol
Functional group
Functional groups -Create the necessary variety of shapes of macromolecules for life to exist
Dehydration synthesis =
enzymatically controlled
formation of large molecules by
removal of water
Macromolecules
• Monomers + monomers + monomers = polymers
• Produced by DEHYDRATION SYNTHESIS
• Hydrolysis – breakdown of macromolecules by the addition of water
• Enzymes
Macromolecules• What do you need to know for each
macromolecule important to life:
– Structure
– Monomers
– Function in organisms
Macromolecules
• Carbohydrates
• Lipids
• Proteins
• Nucleic acids
Carbohydrates
• Carbon + water (hydrate)
• Basic formula: CH2O(n)
• Monomers = monosaccharide (‘one sugar’)
• End in ‘ose’
Monosaccharides
• Glucose C6H12O6
• Many monomers form rings in aqueous solutions to become more stable
• Monomers may be functional:
– Glucose is primary source of energy for organisms
Carbohydrates• Monomer + monomer = dimer• Monosaccharide + monosaccharide = disaccharide • Glucose + glucose = maltose• Glucose + fructose = sucrose• Glucose + galactose = lactose
Polysaccharides
• Polymers of monosaccharides
• Type of monosaccharide and arrangement creates variation in polysaccharides
• Starch (Amylose, amylopectin) = plants
• Glycogen = energy storage for animals
• Cellulose = plant cell walls
• Chitin = exoskeleton of arthropods, some fungi
Carbohydrates: Function
• Energy; stored energy (which?)
• Structure – (which?)
• Cell-to-cell communication, identification (glycoproteins, glycolipids)
– Antigens /antibodies
Lipids • InsolubleInsoluble in water; (long, nonpolar
hydrocarbon chains) • Basic formula: C50H70O6
• Three types:– Fats, oils, waxes– Phospholipids – Steroids
Lipids: Fats
• Macromolecules of glycerol + 3 fatty acids
• Glycerol = glyc = ‘sugar’ C3H8O3
• Fatty acids = hydrocarbon chain (16-18 carbons)– Hydrocarbon chain is hydrophobic
Lipids: Fats
• Fats = triglycerides (3 fatty acids)
• Structure of the fatty acid chains creates variety in types of fats
– Saturated – full of hydrogen atoms; no double bonds
– Unsaturated – not full; double bond(s)
Types of Fats
• Saturated
• No double bonds• Saturated• Solids @ (200)• Animal fats• Bacon grease, lard,
butter
• Unsaturated • Double bond(s)• Unsaturated• Liquids @ (200)• Plant fats (oil)• Corn, peanut, olive
oils
Link between an acid and a sugar
Triglycerides
• Important to diet
• Limit amount of saturated fats
• Hydrocarbon chains are high in energy
• More difficult to breakdown
• Link to triglycerides and arteriosclerosis
Lipids: Phospholipids
• Glycerol + 2 fatty acids • 3rd position on the glycerol is taken by a phosphate
group (PO4)
Phospholipids
• Major component of cell membrane
• ‘head’ end (glycerol) is polar (term?)• Hydrophilic = “water loving”• ‘tail’ end is non-polar (term?)• Hydrophobic = “water fearing”
Phospholipids• Phospholipids in water form a micelle
• First prokaryotes evolved when phospholipids formed micelles in water (?)
• Abiogenesis
Steroids
• 4 fused carbon rings + functional group
• Insoluble in water
• Ex. Cholesterol
– Between fatty acids tails of phospholipids
– Help to moderate the effects of extreme temperatures
Steroids
• Precursors of sex hormones
• Too much causes atherosclerosis (?)
Importance
• Energy (?)• Padding (?)• Insulation (?)• Structure (?)• Hormones (?)
Proteins
• Many shapes = many functions
• ‘first place’
• Polymers of AMINO ACIDS
• Linked by PEPTIDE BONDS
• POLYPEPTIDES
• Proteins = folded, shaped polypeptides
Proteins: Amino Acids
• 2 carbon skeleton
– Amino group
– Carboxyl group
– H atom
• Side group (R group)
Proteins: Amino Acids
• R group determines properties of the aa– Some are polar, some are nonpolar– Polar may be acidic or alkaline
• 20 different amino acids• Essential = body cannot produce on its own
Proteins
• Peptide bonds are the result of dehydration synthesis
• Amino group reacts with carboxyl group of adjacent amino acid
• Polypeptide - string of polypeptide bonds
Proteins• Function depends upon shape
• Conformation – 3d shape caused by H-bonds
– Fold and twist the amino acids
• Globular
– Insulin, enzymes
• Fibrous = ‘stringy’
– Silk, muscle
Proteins
• Four levels of protein structure that give a protein its unique shape:
– Primary
– Secondary
– Tertiary
– Quaternary
Proteins: Primary Structure
• Sequence of amino acids
– Determined by genetic code
– ‘goof’ in sequence can have harmful or lethal effects
Secondary Structure
• Folds or twists created by H-bonding in the carbon backbone; NOT the R group
• 2 types: both may be in a protein – Alpha - helix – Beta - pleated sheet
Tertiary Structure• Irregular contortions caused
by bonding of R groups:– Ionic, hydrogen, disulfide
bridges (covalent)• Hydrophobic interaction -
nonpolar portions tend to line up in core of the protein
Quaternary Structure
• Multiple polypeptides in one giant protein
– Hemoglobin (heme + globin)
Protein Shape
• Primary – (?)• Secondary – (?)• Tertiary – (?) • Quaternary – (?)
Denaturation
• Alteration of conformational shape
• Caused by:
– pH, salinity, organic solvents (alcohols, carbon tetrachloride, acetone, etc.), heat, inorganic chemicals that dissolve bonds (HCl)
• Some change shape to function
– Receptor, contractile
Denatured proteins are the cause of….
Polypeptide to Protein
• Polypeptides are NOT proteins– Need to be folded into conformational
shape• Chaperonins = proteins that aid in the
folding into conformational shape• Knowledge of protein folding helps to
manufacture proteins
Determining the Structure of Molecules
• X-ray diffraction
• Electron density map
• Computer
Rosalind Franklin: X-ray diffraction of
DNA
Nucleic Acids
• DNA, RNA
• Polymers of nucleotides
• Nucleotide:
– Simple sugar (ribose or deoxyribose)
– Nitrogenous base
– Phosphate group (PO3)
4 nitrogenous bases: Purines Pyrimidines
Nucleic Acids
• Nitrogenous bases are complimentary
• A-T
• C-G
• Hydrogen bonds
• Sugar-phosphate backbone
H bonding
Relationship between
nucleic acids and proteins