ch4_7-11 - Chapter 4 Objectives (7-11) 7. Define native...

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Chapter 4 Objectives (7-11) 7. Define native protein, denature protein, renatured protein; list conditions under which globular proteins may be denatured and renatured, using ribonuclease as a model; describe molecular chaperones and protein disulfide isomerases and their roles in protein folding; discuss the protein folding process, diving it into early, intermediate, and final stages. Native conformation is the biologically active conformation of a macromolecule, such as a protein. A denatured protein has lost its native conformation by exposure to a destabilizing agent. Destabilizing agents include heat, pH extremes, organic solvents, high concentrations of salts, detergents, and H- bond breaking reagents such as urea. Renaturation is the refolding of a denatured protein to restore native structure and functional activity.
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  Early events   - local secondary structures ( ) formed αα αβ ββ       - hydrophobic collapse with expulsion of water   Intermediate stage       - secondary structure stabilized
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This note was uploaded on 05/01/2011 for the course CHEMISTRY 410 taught by Professor Bayse during the Spring '11 term at Spelman.

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ch4_7-11 - Chapter 4 Objectives (7-11) 7. Define native...

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