MICR 303 Lecture Notes - Lecture 2: Hydrophile, Acid Dissociation Constant, Glyceraldehyde
Document Summary
Starts w/ 20 amino acids (chemically reactive and distinct) Same core structure but side-chains = chemically distinct. Most reactions catalyzed by proteins (most enzymes are proteins (some are not -> protein production in ribosome catalyzed by rna) Proteins structure determines function (if you denature -> disrupt function) Structure determined by composition of amino acids. Important terms: a. a = amino acid residue = amino acid protein = polypeptide oligopeptide = small protein. > determined by interaction of hydrophobic components with aqueous environment or the non- polar interactions with polar environment. Proteins are polar -> n = + terminus, c = - terminus. Modi cation can cause branching (but will see in 300b) Polypeptide chain (primary structure, linear sequence, etc. ) Unique and recurring group of small structural entities. Spacial relationship among all amino acids in polypeptide. Doesn"t happen for all but if more than on polypeptide in structure -> how they interact with each other determines quaternary structure (dimeric, trimeric, etc. )