Intramolecular alpha-helix-beta-structure-random coil transition in polypeptides. I. Equilibrium case
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Updated: Jul 19, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
1Department of Applied Physics, School of Science and Engineering, Waseda University, Okubo, Tokyo 160, Japan.
Abstract:
The present paper is devoted to the study of the conformational transition of polypeptides which are capable of forming alpha-helix, beta-structure and random coil conformations with the finite homogeneous chain model. The experimental results on the surfactant-induced conformational change of poly(L-lysine) can be well described by the present model assuming cooperative binding of the surfactant ions to the polypeptide side groups.
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