論文

査読有り 国際誌
2002年4月

A pH-dependent variation in α-helix structure of the S-peptide of ribonuclease a studied by Monte Carlo simulated annealing

Biopolymers
  • Takashi Nakazawa
  • ,
  • Sumiko Ban
  • ,
  • Yuka Okuda
  • ,
  • Masato Masuya
  • ,
  • Ayori Mitsutake
  • ,
  • Yuko Okamoto

63
4
開始ページ
273
終了ページ
279
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1002/bip.10055
出版者・発行元
JOHN WILEY & SONS INC

Low-energy conformations of the S-peptide fragment (20 amino acid residues long) of ribonuclease A were studied by Monte Carlo simulated annealing. The obtained lowest-energy structures have α-helices with different size and location, depending distinctively on the ionizing states of acidic amino acid residues. The simulation started from completely random initial conformation and was performed without any bias toward a particular structure. The most conspicuous a-helices arose from the simulation when both Glu 9 and Asp 14 were assumed to be electrically neutral, whereas the resulting conformations became much less helical when Asp 14 rather than Glu 9 was allowed to have a negative charge. Together with experimental evidence that the a-helix in the S-peptide is most stable at pH 3.8, we consider the helix formation need the carboxyl group of Asp 14 to be electrically neutral in this weakly acidic condition. In contrast, a negative charge at Asp 14 appears to function in support of a view that this residue is crucial to helix termination owing to its possibility to form a salt bridge with His 12. These results indicate that the conformation of the S-peptide depends considerably on the ionizing state of Asp 14. © 2002 John Wiley & Sons, Inc.

リンク情報
DOI
https://doi.org/10.1002/bip.10055
CiNii Articles
http://ci.nii.ac.jp/naid/80015400058
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/11807754
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000173990000006&DestApp=WOS_CPL
Scopus
https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0037023670&origin=inward
Scopus Citedby
https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=0037023670&origin=inward
ID情報
  • DOI : 10.1002/bip.10055
  • ISSN : 0006-3525
  • CiNii Articles ID : 80015400058
  • PubMed ID : 11807754
  • SCOPUS ID : 0037023670
  • Web of Science ID : WOS:000173990000006

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