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2015年07月31日 掲載 (Published 07/31/2015)


「Biophysics and Physicobiology」に Koji Oda et al."Physicochemical origin of high correlation between thermal stability of a protein and its packing efficiency: a theoretical study for staphylococcal nuclease mutants "を掲載

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Koji Oda and Masahiro Kinoshita
"Physicochemical origin of high correlation between thermal stability of a protein and its packing efficiency: a theoretical study for staphylococcal nuclease mutants "


【Significance】
The factor determining the structural stability of a protein against heating, cooling, and raising pressure.

The thermal stability of a protein is not correlated with the number of intramolecular hydrogen bonds, intramolecular electrostatic interaction energy, or degree of burial of the hydrophobic surface in the folded state. Seemingly, it is correlated with the number of van der Waals contacts (factor 1). Truly, it is correlated with the water-entropy gain upon folding (factor 2). Cold and pressure denaturation can also be elucidated by a theory emphasizing not factor 1 but factor 2. Looking at thermal denaturation alone is inadequate to determine the true physical factor governing the structural stability of a protein.


Biophysics and Physicobiology, Vol.12, pp. 1-12
URL:http://doi.org/10.2142/biophysico.12.0_1