BCHM 310- Final Exam Guide - Comprehensive Notes for the exam ( 26 pages long!)
30 Nov 2017
School
Department
Course
Professor
Document Summary
You are also going to influence the backbone carbonyl groups; these carbonyl groups are going to have ionization states. You are disrupting electrostatic interactions and hydrogen bonds. Recall hydrogen bonds stabilize secondary structures -- but at the same time you have a lot of electrostatic interactions. The best method for us to manipulate fold and unfoldinf is to use chaotropic agents: ex: urea, guanidine salts; don"t need a high concentration to do this. The reason these salts work is that they can h-bond with the protein and stabilize/ solubilize the unfolded state. The hydrophobic effect is really what is driving the formation of the core to the protein. In order to renature or refold the protein to its native (folded) state, you dialyze into native buffer conditions. The dialysis tubing is porous, your protein is too big to pass through,, but you get movement out of the bag of urea until it reaches equilibrium.
