Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back.
Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back.
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DOI：
10.1146/annurev-physchem-032210-103531
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发表时间：
2011
影响因子：
14.7
通讯作者：
Haran G
中科院分区：
文献类型：
--
作者：
England JL;Haran G
通常通过使用尿素和氯化胍（破坏蛋白质天然结构的化学共溶剂）在体外研究蛋白质稳定性。围绕这些分子使蛋白质变性的潜在机制仍然存在很多争议。在这里，我们回顾了当前对化学变性各个方面的思考。我们首先讨论蛋白质折叠的经典模型，以及变性剂的影响如何通过其对塌缩或卷曲球转变（通常在折叠之前）的调节来适应这一情况。随后，我们研究了最近的分子动力学模拟，这些模拟为变性剂引起的溶剂化效应的可能微观起源提供了新的线索。两种变性剂似乎都是通过促进蛋白质疏水区域的溶剂化来起作用的。最后，我们介绍了最近对变性蛋白质的单分子荧光研究，其分析证实了变性剂在改变线圈-球体转变平衡中的作用。
Protein stability often is studied in vitro through the use of urea and guanidinium chloride, chemical cosolvents that disrupt protein native structure. Much controversy still surrounds the underlying mechanism by which these molecules denature proteins. Here we review current thinking on various aspects of chemical denaturation. We begin by discussing classic models of protein folding and how the effects of denaturants may fit into this picture through their modulation of the collapse, or coil-globule transition, which typically precedes folding. Subsequently, we examine recent molecular dynamics simulations that have shed new light on the possible microscopic origins of the solvation effects brought on by denaturants. It seems likely that both denaturants operate by facilitating solvation of hydrophobic regions of proteins. Finally, we present recent single-molecule fluorescence studies of denatured proteins, the analysis of which corroborates the role of denaturants in shifting the equilibrium of the coil-globule transition.
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DOI：
10.1073/pnas.0404236101
发表时间：
2004-08-24
影响因子：
11.1
作者：
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通讯作者：
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影响因子：
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影响因子：
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DOI：
10.1073/pnas.0706251104
发表时间：
2007-09-25
影响因子：
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作者：
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