Forces stabilizing proteins.
Forces stabilizing proteins.
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DOI：
10.1016/j.febslet.2014.05.006
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发表时间：
2014-06-27
期刊：
影响因子：
3.5
通讯作者：
Grimsley GR
中科院分区：
文献类型：
--
作者：
Nick Pace C;Scholtz JM;Grimsley GR
本文的目的是总结自20世纪80年代后期定点突变成为可能以来，人们对稳定蛋白质的主要力量的了解。以下结论来自疏水和氢键变体的实验研究。1.基于对11种蛋白质中138种疏水相互作用变体的研究，在折叠上掩埋-CH 2-基团对蛋白质稳定性的贡献为1.1 ± 0.5 kcal/mol。2.非极性侧链的掩埋以两种方式对蛋白质稳定性做出贡献：第一，取决于从水中去除侧链的术语，更重要的是，由蛋白质内部的紧密包装引起的增强的伦敦分散力。3.基于对15种蛋白质中151种氢键变体的研究，折叠时形成氢键对蛋白质稳定性的贡献为1.1 ± 0.8 kcal/mol。4.氢键对蛋白质稳定性的贡献是强烈依赖于上下文的。5.侧链和肽基团的氢键对蛋白质稳定性做出类似的贡献。6.即使极性基团不是氢键键合的，极性基团掩埋也可以对蛋白质稳定性做出有利的贡献。7.疏水相互作用和氢键都对蛋白质的稳定性有很大的贡献。
The goal of this article is to summarize what has been learned about the major forces stabilizing proteins since the late 1980s when site-directed mutagenesis became possible. The following conclusions are derived from experimental studies of hydrophobic and hydrogen bonding variants. 1. Based on studies of 138 hydrophobic interaction variants in 11 proteins, burying a –CH2– group on folding contributes 1.1 ± 0.5 kcal/mol to protein stability. 2. The burial of nonpolar side chains contributes to protein stability in two ways: first, a term that depends on the removal of the side chains from water and, more importantly, the enhanced London dispersion forces that result from the tight packing in the protein interior. 3. Based on studies of 151 hydrogen bonding variants in 15 proteins, forming a hydrogen bond on folding contributes 1.1 ± 0.8 kcal/mol to protein stability. 4. The contribution of hydrogen bonds to protein stability is strongly context dependent. 5. Hydrogen bonds by side chains and peptide groups make similar contributions to protein stability. 6. Polar group burial can make a favorable contribution to protein stability even if the polar group is not hydrogen bonded. 7. Hydrophobic interactions and hydrogen bonds both make large contributions to protein stability.
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