Side-chain Conformations Cooperatively Restricted in Protein Secondary Structure : II. Side-chain Configurational Entropies of α-helices in the Folding Nuclei
スポンサーリンク
概要
- 論文の詳細を見る
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.
- 日本学士院の論文
著者
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Kidera Akinori
Biomolecular Engineering Research Institute
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NAKAMURA Haruki
Biomolecular Engineering Research Institute
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Kidera Akinori
Graduate school of nanobioscience, Yokohama city university
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Nakamura H
Osaka Medical Center For Cancer & Cardiovascular Diseases Osaka Jpn
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TANIMURA Ryuji
Basic Research Laboratories, Toray Industries, Inc.
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Kidera Akinori
Graduate School Of Nanobioscience Yokohama City University:research Program For Computational Scienc
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KIDERA Akinori
Graduate School of Science, Kyoto University
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