BISC207 Chapter Notes - Chapter 3: Motor Protein, Antibody, Protein Folding

• School: University of Delaware
• Department: Biological Sciences
• Course: BISC207
• Professor: Nauen Jennifer

Document Summary

Unfolded protein have much higher entropy than the folded version. Folding does seem to be spontaneous due to chemical bonds that releases enough energy to overcome desire in entropy and will also increase entropy in surrounding environment. As a result, folded molecule has less potential energy and is thus more stable than unfolded molecule. Can be done by treating it w compounds that break h bonds and disulfide bonds. If chemical denaturing agents removed, protein can refold and begin to function properly again. Cells contain proteins called molecular chaperones that can facilitate protein folding. When not actively performing, can maintain a flexible shape. Certain normal proteins can be induced to fold into infectious, disease carrying agents. These infectious and normal proteins do not differ in their primary structure, but their shapes are radically dif. 3. 4 protein functions are as diverse as protein structures.