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关于蛋白质折叠的熵

On the entropy of protein folding.

作者信息

Makhatadze G I, Privalov P L

机构信息

Department of Biology and Biocalorimetry Center, Johns Hopkins University, Baltimore, Maryland 21218, USA.

出版信息

Protein Sci. 1996 Mar;5(3):507-10. doi: 10.1002/pro.5560050312.

Abstract

The failure to appreciate that the hydration of polar groups is a major contribution to the entropy of protein unfolding has led to considerable underestimates for the loss of configurational freedom when a protein chain folds.

摘要

未能认识到极性基团的水合作用对蛋白质展开熵有重大贡献,导致在蛋白质链折叠时对构型自由度损失的严重低估。

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本文引用的文献

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Energetics of protein structure.蛋白质结构的能量学
Adv Protein Chem. 1995;47:307-425. doi: 10.1016/s0065-3233(08)60548-3.
6
Structural basis of amino acid alpha helix propensity.氨基酸α-螺旋倾向的结构基础。
Science. 1993 Jun 11;260(5114):1637-40. doi: 10.1126/science.8503008.
10
Thermodynamics of ubiquitin unfolding.泛素去折叠的热力学
Proteins. 1994 Mar;18(3):246-53. doi: 10.1002/prot.340180305.

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