Theoretical analysis on thermal stability of a protein focused on the water entropy

Ken ichi Amano, Takashi Yoshidome, Yuichi Harano, Koji Oda, Masahiro Kinoshita

研究成果: Article査読

33 被引用数 (Scopus)

抄録

We have recently shown that the water entropy is the key quantity in elucidating the folding/unfolding mechanisms for proteins. Here we consider thermal denaturation. The water-entropy gain upon the transition from the random-coil state to the native structure is calculated for some representative proteins by employing the angle-dependent integral equation theory combined with the multipolar water model and the morphometric approach. It is found that the water-entropy gain at 25 °C divided by the number of residues is a good measure of the thermal stability. A protein with a larger value of this measure tends to have a higher denaturation temperature.

本文言語English
ページ(範囲)190-194
ページ数5
ジャーナルChemical Physics Letters
474
1-3
DOI
出版ステータスPublished - 2009 5 25
外部発表はい

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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