BIOL 2020 Study Guide - Final Guide: Amide, Polyacrylamide Gel Electrophoresis, Peptide Bond
Document Summary
Knowing the primary sequence of aa"s are good because (4) Most proteins are __ to __ in size. Describe the use of gel electrophoresis, type of gel, and how the proteins are separated. What is known about peptide chains flexibility? (4) Aa sequence, 3d structure from the n-h &c-h bonds, r groups bonding (intramolecular), more than one polypeptide chain(inter and intra) small are oligopeptides or peptides. 3d structure is determined by it, eludicating its mechanism, medical reasons (point mutations or misfolds e. g. cystic fibrosis or sickle cell), knowing evolutionary history. Amino end (beginning) and carboxyl end have different charges, and peptide bond has partial double bonding. Hydrocarbons, hydrogen bond acceptor and can interact with each other and functional groups from side chains. Titin, 27,000 aa and is a contractile muscle scaffold. Called a cystine can be same chain or different, just in close proximity.
