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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.

DOI:10.1002/pro.5560050312
PMID:8868487
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2143355/
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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Some factors in the interpretation of protein denaturation.蛋白质变性解读中的一些因素。
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Energetics of protein structure.蛋白质结构的能量学
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Structural energetics of peptide recognition: angiotensin II/antibody binding.肽识别的结构能量学:血管紧张素II/抗体结合
Proteins. 1993 Feb;15(2):113-20. doi: 10.1002/prot.340150203.
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Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration.水合作用对蛋白质折叠热力学的贡献。II. 水合作用的熵和吉布斯自由能。
J Mol Biol. 1993 Jul 20;232(2):660-79. doi: 10.1006/jmbi.1993.1417.
9
Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.在折叠蛋白背景下测定α-螺旋倾向。噬菌体T4溶菌酶中的44位和131位。
J Mol Biol. 1994 Jan 14;235(2):600-24. doi: 10.1006/jmbi.1994.1016.
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.