BSC 2010 Lecture Notes - Lecture 5: Hydrogen Bond, Titin, Oligopeptide
31 Aug 2016
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Lecture 5 nucleic acids, proteins, and enzymes a. i. There are only 20 different amino acids in proteins of organisms a. ii. Grouped according to properties of r groups a. iii. Oligopeptide or peptides short polymers of 20 or fewer amino acids a. iv. Linked in condensation reactions to form peptide linkages a. iv. 1. Polymerization takes place in the amino to carboxyl direction: proteins are polymers with important structural and metabolic roles b. i. Polypeptides (proteins) range in size from insulin (51 amino acids) to huge molecules such as the muscle protein titin (34,350 amino acids) b. iii. Secondary regular, repeated spatial patterns in different regions (results from hydrogen bonding) b. iii. 2. a. Two types of secondary structure b. iii. 2. a. i. a (alpha) helix right handed coil b. iii. 2. a. ii. (beta) pleated sheet two or more polypeptide chains are extended and aligned b. iii. 3. Final, folded, 3-d shape of a polypeptide b. iii. 3. b. Determined by interactions between r groups rather than between backbone constituents b. iii. 3. b. i. Disulfide bridges hold the folded polypeptide together b. iii. 3. b. ii.
