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首页> 外文期刊>Journal of Molecular Biology >Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different
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Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different

机译：作为展开蛋白质的良好溶剂的水：折叠和崩溃是根本不同的

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摘要

The argument that the hydrophobic effect is the primary effect driving the folding of globular proteins is nearly universally accepted (including by the authors). But does this view also imply that water is a "poor" solvent for the unfolded states of these same proteins? Here we argue that the answer is "no," that is, folding to a well-packed, extensively hydrogen-bonded native structure differs fundamentally from the nonspecific chain collapse that defines a poor solvent. Thus, the observation that a protein folds in water does not necessitate that water is a poor solvent for its unfolded state. Indeed, chain-solvent interactions that are marginally more favorable than nonspecific intrachain interactions are beneficial to protein function because they destabilize deleterious misfolded conformations and inter-chain interactions. (C) 2020 Elsevier Ltd. All rights reserved.
机译：疏水效应是推动球状蛋白折叠的主要效果几乎普遍接受（包括作者）。 但这侧面还暗示，水是对这些相同蛋白质的展开状态的“差”溶剂？ 在这里，我们认为答案是“不”，也就是说，折叠到填充良好的，广泛的氢键的天然结构的根本不同于定义溶剂的非特异性链塌陷。 因此，观察到蛋白质在水中折叠不需要水是其展开状态的差的溶剂。 实际上，链溶剂相互作用比非特异性内衣相互作用更良好地对蛋白质功能有益，因为它们破坏了有害错误折叠的构象和间歇性相互作用。 （c）2020 elestvier有限公司保留所有权利。

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