LIFESCI 3 Lecture Notes - Lecture 7: Van Der Waals Force, Christian B. Anfinsen, Protein Folding

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12 Mar 2018
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Hydrophobic effect: lowest energy state is most often attained with hydrophobic aa buried & hydrophilic aa exposed: 5 factors promoting protein folding & stability. 3. ) disulfide bridge covalent crossing, locks structure into place, disulfide bonds form an oxidizing environment. 5. ) ionic bonds bonding negative & positive charges for stability: christian anfinsen experiment: aa sequence is sufficient to determine 3rd structure (slide) native structure of protein --> denatures, reduce --> denatured protein --> 1. ) remove denaturant & reducing agent together or 2. ) removing reducing agent and then remove denaturant --> 1. ) native or. Denature protein: needs a special reducing agent to break up disulfide bonds: protein folding. Spontaneous folding: most proteins can fold to native form spontaneously. Chaperone-assisted folding: chaperone proteins required for proper folding of some polypeptide chains. Binds to unfolded polypeptides to prevent aggregation can also help unfold mistakes.

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