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Transcript
Protein folding reading: Creighton sections 7.1, 7.3, 7.4 and 7.5 The nature of the unfolded state Not completely random. Molten globule state: Creighton pg 292 Denaturants: Urea Guanidinium Chloride Temperature pH Other solvents Most common chemical denaturants used in protein folding studies Effects of additives to protein solutions Effects of some organic solvents Increase solubility of polar and nonpolar side chains Effects of the counter anion Absorbance Aromatic amino acid residues absorb strongly Folding transitions Transverse urea gradient electrophoresis Can obtain DG directly from the data Thermal denaturation Need to obtain T* and DH* DG for different proteins Cooperative versus noncooperative folding Simulated Sequential mechanism: U -> I1 -> I2 -> N Linked functions The folding pathway for BPTI
