Chapter 4: PROTEIN SYNTHESIS

Chapter 3: PROTEIN STRUCTURE & FUNCTION

Amino acids and protein structure:

Structural groups of amino acids (3-2); primary structure of proteins (3-3); secondary structures (a -helix, b sheet, random coil) (3-6,3-8); tertiary structure - motifs of secondary structures (3-9); disulfide bonds (3-13); quaternary structure (3-4).
Protein folding (3-14); Chaperones promote proper folding (3-15).
Protein degradation; extracellular degradation by digestive proteases; lysosomal pathway; ubiquitin mediated proteolysis (3-18).

Protein function:

Function generally depends on binding of to ligands; binding is dependent on affinity and specificity.
Enzyme function — catalysis of reactions that convert substrates to products; active site and catalysis by stabilizing the transition state (3-23, 3-24); catalysis is described by the affinity of an enzyme for substrate (K_m) and the maximal velocity of a reaction in saturating amounts of substrate (V_max).
Regulating protein function; allosteric release of catalytic subunits (3-27); allosteric transition between active and inactive states (3-28); cooperative binding of ligands (hemoglobin binding to oxygen); phosphorylation; proteolytic activation (3-31).