BIOLOGY 2B03 Study Guide - Midterm Guide: Heat Shock Protein, Atp Hydrolysis, Hsp70

• School: McMaster University
• Department: Biology
• Course: BIOLOGY 2B03
• Professor: Suleiman A Igdoura

Document Summary

Identify principles for helping proteins fold: describe mechanisms employed by molecular chaperones/chaperonin, 2 step process required for protein degradation, correcting misfolding: chaperones, most proteins fold rapidly on their own. If they misfold or unfold chaperones assist in folding: by preventing inappropriate interactions, misfolding aggregation. If aggregates form degradation in proteasome: 2 types of chaperones, monomeric molecular chaperone, bind to hydrophobic a. a residues on a polypeptide, prevent proteins from incorrect folds due to hydrophobic interaction in an aqueous environment, ex. Recorded lecture 2: regulation and function: objectives. Identify properties that determine affinity and specificity of protein-substrate interactions: examine enzyme kinetics and identify ways of calculating affinity. [(cid:2168)][: where [lp] is the concentration of the ligand protein complex. Conformation change: pseudo-substrate unit changes shape and no longer binds to pka. Catalytic site is removed from pka active enzyme. [camp] regulates activity of enzyme: more [camp] more active; vise versa for less [camp, sub-units of pka, catalytic sub-unit: protein folded into c-shape.