Structure-based analysis reveals hydration changes induced by arginine hydrochloride

Makoto Nakakido, Yoshikazu Tanaka, Mariko Mitsuhori, Motonori Kudou, Daisuke Ejima, Tsutomu Arakawa, Kouhei Tsumoto

研究成果: Article

16 引用 (Scopus)

抜粋

Arginine hydrochloride has been used to suppress protein aggregation during refolding and in various other applications. We investigated the structure of hen egg-white lysozyme (HEL) and solvent molecules in arginine hydrochloride solution by X-ray crystallography. Neither the backbone nor side-chain structure of HEL was altered by the presence of arginine hydrochloride. In addition, no stably bound arginine molecules were observed. The number of hydration water molecules, however, changed with the arginine hydrochloride concentration. We suggest that arginine hydrochloride suppresses protein aggregation by altering the hydration structure and the transient binding of arginine molecules that could not be observed.

元の言語English
ページ(範囲)105-109
ページ数5
ジャーナルBiophysical Chemistry
137
発行部数2-3
DOI
出版物ステータスPublished - 2008 10 1
外部発表Yes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Organic Chemistry

フィンガープリント Structure-based analysis reveals hydration changes induced by arginine hydrochloride' の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。

  • これを引用

    Nakakido, M., Tanaka, Y., Mitsuhori, M., Kudou, M., Ejima, D., Arakawa, T., & Tsumoto, K. (2008). Structure-based analysis reveals hydration changes induced by arginine hydrochloride. Biophysical Chemistry, 137(2-3), 105-109. https://doi.org/10.1016/j.bpc.2008.07.009