論文

査読有り
2018年4月12日

Analysis of Structural Stability of Chignolin

Journal of Physical Chemistry B
  • Yutaka Maruyama
  • ,
  • Ayori Mitsutake

122
14
開始ページ
3801
終了ページ
3814
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1021/acs.jpcb.8b00288
出版者・発行元
American Chemical Society

We discuss the stability of an entire protein and the influence of main chains and side chains of individual amino acids to investigate the protein-folding mechanism. For this purpose, we calculated the solvation free-energy contribution of individual atoms using the three-dimensional reference interaction site model with the atomic decomposition method. We generated structures of chignolin miniprotein by a molecular dynamics simulation and classified them into six types: native 1, native 2, misfolded 1, misfolded 2, intermediate, and unfolded states. The total energies of the native (-171.1 kcal/mol) and misfolded (-171.2 kcal/mol) states were almost the same and lower than those of the intermediate (-158.5 kcal/mol) and unfolded (-148.1 kcal/mol) states
however, their components were different. In the native state, the side-chain interaction between Thr6 and Thr8 is important for the formation of π-turn. On the other hand, the hydrogen bonds between the atoms of the main chains in the misfolded state become stronger than those in the intermediate state.

Web of Science ® 被引用回数 : 6

リンク情報
DOI
https://doi.org/10.1021/acs.jpcb.8b00288
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/29526100
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000430641900013&DestApp=WOS_CPL
ID情報
  • DOI : 10.1021/acs.jpcb.8b00288
  • ISSN : 1520-5207
  • ISSN : 1520-6106
  • PubMed ID : 29526100
  • SCOPUS ID : 85045459481
  • Web of Science ID : WOS:000430641900013

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