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

Len Ito, Kentaro Shiraki, Takanori Matsuura, Masaki Okumura, Kazuya Hasegawa, Seiki Baba, Hiroshi Yamaguchi, Takashi Kumasaka

研究成果: Article査読

70 被引用数 (Scopus)

抄録

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-π 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.

本文言語English
ページ(範囲)269-274
ページ数6
ジャーナルProtein Engineering, Design and Selection
24
3
DOI
出版ステータスPublished - 2011 3月
外部発表はい

ASJC Scopus subject areas

  • バイオテクノロジー
  • バイオエンジニアリング
  • 生化学
  • 分子生物学

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