BCH210H1 Lecture Notes - Lecture 6: Alpha Helix, Pancreatic Ribonuclease, Ribonuclease

• School: UTSG
• Department: Biochemical Engineering and Applied Chemistry
• Course: BCH210H1
• Professor: Wright

Document Summary

Takes 103 to 10-1 sec to fold protein folding is direct. Folding is not random, dedicate by the aa found in the linkage, Phi and psi angle restrict the way the proteins fold. Anfinsen"s postulate: primary sequences determines the secondary and tertiary. Disulfide bonds stabilizes the folded structure of ribonucleases. Cys residue is not in the order of the sequence, it folds and the disulfide bond is formed. Example: cys110-cys57 far apart in the linkage but when fold they are close enough to link together. Mercaptoethanol = oh-ch 2 ch 2 -sh (breaks the disulfide bonds disrupts the structure) Found that the reduced rnas (using -mer) unfolds completely only when the protein is also treated with denaturing agents (urea or guanidine) Ie. primary structure determines secondary and tertiary structures. Breaks the h bond disrupts 2 o structures. Diminishes the hydrophobic effect reduces the activity in water. Denaturing can be done with urea and -mercaptoethanol.