論文

査読有り
2011年3月

High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine

PROTEIN ENGINEERING DESIGN & SELECTION
  • Len Ito
  • ,
  • Kentaro Shiraki
  • ,
  • Takanori Matsuura
  • ,
  • Masaki Okumura
  • ,
  • Kazuya Hasegawa
  • ,
  • Seiki Baba
  • ,
  • Hiroshi Yamaguchi
  • ,
  • Takashi Kumasaka

24
3
開始ページ
269
終了ページ
274
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1093/protein/gzq101
出版者・発行元
OXFORD UNIV PRESS

While biotechnological applications of arginine (Arg) as a solution additive that prevents protein aggregation are increasing, the molecular mechanism of its effects remains unclear. In this study, we investigated the Arg-lysozyme complex by high-resolution crystallographic analysis. Three Arg molecules were observed to be in close proximity to aromatic amino acid residues of the protein surface, and their occupancies gradually increased with increasing Arg concentration. These interactions were mediated by electrostatic, hydrophobic and cation-pi interactions with the surface residues. The binding of Arg decreased the accessible surface area of aromatic residues by 40%, but increased that of charged residues by 10%. These changes might prevent intermolecular hydrophobic interactions by shielding hydrophobic regions of the lysozyme surface, resulting in an increase in protein solubility.

Web of Science ® 被引用回数 : 62

リンク情報
DOI
https://doi.org/10.1093/protein/gzq101
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/21084280
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000287486500004&DestApp=WOS_CPL
URL
http://www.scopus.com/inward/record.url?eid=2-s2.0-79551498658&partnerID=MN8TOARS
URL
http://orcid.org/0000-0003-2001-9537

エクスポート
BibTeX RIS