Biology 1002B Lecture 3: Protein Folding Lecture Jan 11
15 Mar 2016
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Document Summary
An enzyme will spontaneously go to its native conformation in an aqueous environment. Measure the catalytic potential of an enzyme. Unfold when you add an denaturant (such as urea very polar) competes for hydrogen bonding groups if urea is at high enough concentration . Protein folding only needs the primary sequence: no cofactors needed or anything. Tertiary sequence is dependent solely on primary sequence. Anfinsen"s dogma does not often apply to real life cells since there may be macromolecule crowding. In vitro . 1mg/ml low concentrations of proteins. In vivo >300mg/ml high concentration of proteins. Polypeptides get in the way of each other: protein folding just doesn"t work interfere. Thousands of proteins that cannot fold properly because of high protein concentration proteins are simple. Assists in the folding, stabilizes non-native forms of protein. Thousands of different types of chaperons to fold different proteins. Interacts with and stabilizes non-native forms of protein.
