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  1. B100 理学部/理学研究科
  2. B100a 雑誌掲載論文
  3. 学術雑誌

Solvation structure and stability of peptides in aqueous solutions analyzed by the reference interaction site model theory

http://hdl.handle.net/2237/00029108
http://hdl.handle.net/2237/00029108
91e65524-5a5b-47a9-8bff-510315d21799
名前 / ファイル ライセンス アクション
1_474511.pdf 1_474511 (8.2 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2018-12-13
タイトル
タイトル Solvation structure and stability of peptides in aqueous solutions analyzed by the reference interaction site model theory
言語 en
著者 Kinoshita, Masahiro

× Kinoshita, Masahiro

WEKO 88171

en Kinoshita, Masahiro

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Okamoto, Yuko

× Okamoto, Yuko

WEKO 88172

en Okamoto, Yuko

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Hirata, Fumio

× Hirata, Fumio

WEKO 88173

en Hirata, Fumio

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利
言語 en
権利情報 Copyright 1997 American Institute of Physics. This article may be downloaded for personal use only. Any other use requires prior permission of the author and AIP Publishing.The following article appeared in (Journal of Applied Physics. v.107, 1997, p.1586-1599) and may be found at (http://dx.doi.org/10.1063/1.474511).
抄録
内容記述 We report results of numerical analyses on solvation structure and conformational stability of a dipeptide and Met-enkephalin in the extended simple point charge (SPC/E) model water. The reference interaction site model (RISM) theory is fully solved using our robust, highly efficient algorithm. It is shown that water structure near the peptides and the hydration free energy are greatly dependent on the peptide conformations. Stability of Met-enkephalin is examined in terms of the total energy defined as the sum of the conformational energy and the hydration free energy of the peptide. We test several different conformations including that with the minimum energy in gas phase, which takes rather compact form due to an intramolecular hydrogen bond. It is shown that a fully extended conformation has the highest stability in water. Our results are in qualitative accord with the recent nuclear magnetic resonance (NMR) experiments which suggest fully extended conformations with large fluctuations for the solution structure of the peptide. A conformation which is similar to that obtained from the NMR experiments in miceller solutions, is much less stable when it is put in water. Thus, the peptide conformations are greatly sensitive to microscopic solvent environment, and any native treatment of the solvent such as the continuum model will end in failure.
言語 en
内容記述タイプ Abstract
出版者
言語 en
出版者 AIP Publishing
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1063/1.474511
ISSN(print)
収録物識別子タイプ PISSN
収録物識別子 0021-9606
書誌情報 en : The Journal of Chemical Physics

巻 107, 号 5, p. 1586-1599, 発行日 1997-08
著者版フラグ
値 publisher
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