Abstract
Conformational analyses for polypeptides having ionizable side chains were carried out by varying side-chain length. The entropy of the chain in the random-coil state was evaluated from the calculated conformational energy. For such acidic polypeptides as poly(L-aspartic acid) and poly(L-glutamic acid), the helix conformation in an ionized state is more stable than in an un-ionized state. On the other hand, with basic polypeptides having long side chains, such as poly(L-lysine), the helix conformation is destabilized by ionization of the side chains. These theoretical results successfully interpret results obtained experimentally on the pH-induced transition of polypeptides.
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Tanaka, S., Nakajima, A. Conformational Aspects of Polypeptides Containing lonizable Side Chains. Polym J 1, 505–517 (1970). https://doi.org/10.1295/polymj.1.505
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DOI: https://doi.org/10.1295/polymj.1.505
