Hydrophobicity at low temperatures and cold denaturation of a protein

Takashi Yoshidome, Masahiro Kinoshita

Research output: Contribution to journalArticlepeer-review

43 Citations (Scopus)

Abstract

We elucidate the microscopic mechanism of the weakening of the hydrophobicity at low temperatures by investigating cold denaturation of a protein. We employ an elaborate statistical-mechanical theory combined with a realistic water model. At low temperatures, the ordered structure with enhanced hydrogen bonds of water molecules is formed near nonpolar groups, leading to entropic loss and energy gain which are both quite large. However, they are canceled out and make no contribution to the free-energy change. We argue that a different factor, which is responsible for the weakening of the hydrophobicity at low temperatures, induces cold denaturation.

Original languageEnglish
Article number030905
JournalPhysical Review E - Statistical, Nonlinear, and Soft Matter Physics
Volume79
Issue number3
DOIs
Publication statusPublished - 2009 Mar 3
Externally publishedYes

ASJC Scopus subject areas

  • Statistical and Nonlinear Physics
  • Statistics and Probability
  • Condensed Matter Physics

Fingerprint Dive into the research topics of 'Hydrophobicity at low temperatures and cold denaturation of a protein'. Together they form a unique fingerprint.

Cite this