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

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

Research output: Contribution to journalArticlepeer-review

35 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)190-194
Number of pages5
JournalChemical Physics Letters
Issue number1-3
Publication statusPublished - 2009 May 25
Externally publishedYes

ASJC Scopus subject areas

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


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