Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.
Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.
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DOI：
10.1016/j.jmb.2020.01.031
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发表时间：
2020-04-17
影响因子：
5.6
通讯作者：
Sosnick TR
中科院分区：
文献类型：
--
作者：
Clark PL;Plaxco KW;Sosnick TR
疏水效应是驱动球形蛋白折叠的主要效应，这一观点几乎被普遍接受（包括作者在内）。但是，这种观点是否也意味着，对于这些蛋白质的未折叠状态来说，水是一种“糟糕的”溶剂？在这里，我们认为答案是否定的。也就是说，折叠成一个包装良好、氢键广泛的天然结构，与定义为不良溶剂的非特异性链坍塌有根本区别。因此，观察到蛋白质在水中折叠并不意味着水是一种不良的溶剂，因为它的未折叠状态。事实上，链-溶剂相互作用比非特异性链内相互作用更有利，有利于蛋白质功能，因为它们破坏了有害的错误折叠构象和链间相互作用的稳定性。
The argument that the hydrophobic effect is the primary effect driving the folding of globular proteins is near 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 non-specific 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 non-specific intra-chain interactions are beneficial to protein function because they destabilize deleterious misfolded conformations and inter-chain interactions.
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影响因子：
6.8
作者：
Chen, Tao;Song, Jianhui;Chan, Hue Sun
通讯作者：
Chan, Hue Sun
影响因子：
8.6
作者：
Adhikari AN;Freed KF;Sosnick TR
通讯作者：
Sosnick TR
DOI：
10.1073/pnas.1209000109
发表时间：
2012-10-23
影响因子：
11.1
作者：
Adhikari, Aashish N.;Freed, Karl F.;Sosnick, Tobin R.
通讯作者：
Sosnick, Tobin R.
影响因子：
5.6
作者：
Baxa, Michael C.;Freed, Karl F.;Sosnick, Tobin R.
通讯作者：
Sosnick, Tobin R.
影响因子：
4.4
作者：
Alborghetti, M. R.;Furlan, A. S.;Kobarg, J.
通讯作者：
Kobarg, J.