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ID 57792
フルテキストURL
著者
Sumi, Tomonari Research Institute for Interdisciplinary Science, Okayama University ORCID Kaken ID publons researchmap
Koga, Kenichiro Research Institute for Interdisciplinary Science, Okayama University ORCID Kaken ID publons researchmap
抄録
Understanding the dominant factor in thermodynamic stability of proteins remains an open challenge. Kauzmann's hydrophobic interaction hypothesis, which considers hydrophobic interactions between nonpolar groups as the dominant factor, has been widely accepted for about sixty years and attracted many scientists. The hypothesis, however, has not been verified or disproved because it is difficult, both theoretically and experimentally, to quantify the solvent effects on the free energy change in protein folding. Here, we developed a computational method for extracting the dominant factor behind thermodynamic stability of proteins and applied it to a small, designed protein, chignolin. The resulting free energy profile quantitatively agreed with the molecular dynamics simulations. Decomposition of the free energy profile indicated that intramolecular interactions predominantly stabilized collapsed conformations, whereas solvent-induced interactions, including hydrophobic ones, destabilized them. These results obtained for chignolin were consistent with the site-directed mutagenesis and calorimetry experiments for globular proteins with hydrophobic interior cores.
発行日
2019-3-26
出版物タイトル
Scientific Reports
9巻
出版者
Nature Publishing Group
開始ページ
5186
ISSN
2045-2322
資料タイプ
学術雑誌論文
言語
English
OAI-PMH Set
岡山大学
著作権者
© The Author(s) 2019
論文のバージョン
Publisher
PubMed ID
DOI
Web of Science KeyUT
関連URL
isVersionOf https://doi.org/10.1038/s41598-019-41518-1
ライセンス
https://creativecommons.org/licenses/by/4.0/
助成機関名
日本学術振興会
助成番号
JP16K05657
JP26287099
JP18KK0151