Side-chain Conformations Cooperatively Restricted in Protein Secondary Structure. II. Side-chain Configurational Entropies of .ALPHA.-helices in the Folding Nuclei.

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  • Side-chain conformations Cooperatively Restricted in Protein Secondary Structure-2-Side-chain Configurational Entropies of α-helices in the Folding Nuclei
  • Side-chain conformations Cooperatively
  • II. Side-chain Configurational Entropies of α-helices in the Folding Nuclei

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Abstract

Protein side-chain configurational entropies and their correlations were analyzed for α-helices in several proteins. The conformations of several bulky side-chains in helices were found to be cooperatively fixed by the restricted side-chain conformations of the neighboring β-branched amino acids. Such helices correspond well to the experimentally observed nuclei in the folding procedures, so that the folding rates should be significantly accerelated. This phenomenon may be a reasonable answer to the Levinthal paradox.

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