Abstract
A statistical mechanical theory on the effects of denaturant on the helix–coil transition of polypeptides was developed. In the proposed theory, unfolding agents were assumed to interact with the polypeptide backbone. The theoretical results were compared with the findings of guanidine-induced helix–coil transition experiments, which were conducted on short peptides (C17 and AK16). Specifically, the helix fraction and average number of helices in C17 and AK16 were estimated. Under unfolding conditions (high denaturant concentration), the number of helices in a given sequence was close to zero. The radius of gyration was measured, and the results were related to those of the proposed theory.
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