Nucleic Acids • DNA, RNA • Instructions for building proteins • Transmit genetic info from one generation to the next
Nucleotides • Sugar, phosphate, nitrogen base – Purine (A, G) two rings – Pyrimidine (C, T) one ring • Held together with phosphodiester linkages b/w sugar and phosphate
Proteins • “You are a constellation of your proteins” • >50% dry mass of most cells • Catalysts, structure, storage transport cellular communication, defense
Amino Acids= monomer • Amino group, carboxyl group, R group • Acidic (-), basic (+), neutral • R groups interact to give protein shape
Polypeptides= polymer • Peptide bonds • N terminus, C terminus
Protein structure • Polypeptides are linear, proteins are 3 D • Structure function – Antibodies, enzymes, receptor proteins • Four levels of structure
Primary Structure • Determined by genetic code
Secondary Structure • Held together by H-bonds – α helix – Β pleated sheet
Tertiary Structure • Interactions between R groups, environment – Hydrophobic interactions – Disulfide bridges
Quaternary Strucuture • Interactions between polypeptide chains
Changes to primary structure
Changes to tertiary structure • Denaturation • Heat, solvents, p. H • Hydrophobic interactions reverse, H-bonds break • Reversible