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本文引用的文献

1
A role for confined water in chaperonin function.受限水在伴侣蛋白功能中的作用。
J Am Chem Soc. 2008 Sep 10;130(36):11838-9. doi: 10.1021/ja802248m. Epub 2008 Aug 19.
2
Potential for modulation of the hydrophobic effect inside chaperonins.伴侣蛋白内部疏水效应的调节潜力。
Biophys J. 2008 Oct;95(7):3391-9. doi: 10.1529/biophysj.108.131037. Epub 2008 Jul 3.
3
Polar confinement modulates solvation behavior of methane molecules.极性限制调节甲烷分子的溶剂化行为。
J Chem Phys. 2008 Jun 21;128(23):234506. doi: 10.1063/1.2940197.
4
Monitoring protein conformation along the pathway of chaperonin-assisted folding.监测伴侣蛋白辅助折叠途径中的蛋白质构象。
Cell. 2008 Apr 4;133(1):142-53. doi: 10.1016/j.cell.2008.01.048.
5
Theory for an order-driven disruption of the liquid state in water.关于水中液态有序驱动破坏的理论。
J Chem Phys. 2008 Jan 28;128(4):044503. doi: 10.1063/1.2823129.
6
Helix formation inside a nanotube: possible influence of backbone-water hydrogen bonding by the confining surface through modulation of water activity.纳米管内的螺旋形成:通过调节水活性,受限表面对主链-水氢键的可能影响。
J Chem Phys. 2007 Dec 28;127(24):245101. doi: 10.1063/1.2812282.
7
Solvent coarse-graining and the string method applied to the hydrophobic collapse of a hydrated chain.溶剂粗粒化与弦方法应用于水合链的疏水塌缩
Proc Natl Acad Sci U S A. 2007 Sep 11;104(37):14559-64. doi: 10.1073/pnas.0705830104. Epub 2007 Aug 28.
8
Protein folding under confinement: a role for solvent.受限环境下的蛋白质折叠:溶剂的作用
Proc Natl Acad Sci U S A. 2007 Jun 19;104(25):10430-4. doi: 10.1073/pnas.0608256104. Epub 2007 Jun 11.
9
Effect of field direction on electrowetting in a nanopore.场方向对纳米孔中电润湿的影响。
J Am Chem Soc. 2007 Mar 7;129(9):2504-10. doi: 10.1021/ja0659370. Epub 2007 Feb 7.
10
Hydrophobic and ionic interactions in nanosized water droplets.纳米水滴中的疏水相互作用和离子相互作用。
J Am Chem Soc. 2006 Oct 18;128(41):13490-6. doi: 10.1021/ja063445h.

荷电、疏水性和受限水:将过去的模拟置于一个简单的理论框架中。

Charge, hydrophobicity, and confined water: putting past simulations into a simple theoretical framework.

机构信息

Department of Physics, Stanford University, Stanford, CA 94305, USA.

出版信息

Biochem Cell Biol. 2010 Apr;88(2):359-69. doi: 10.1139/o09-187.

DOI:10.1139/o09-187
PMID:20453936
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5328680/
Abstract

Water permeates all life, and mediates forces that are essential to the process of macromolecular self-assembly. Predicting these forces in a given biological context is challenging, since water organizes itself differently next to charged and hydrophobic surfaces, both of which are typically at play on the nanoscale in vivo. In this work, we present a simple statistical mechanical model for the forces water mediates between different confining surfaces, and demonstrate that the model qualitatively unifies a wide range of phenomena known in the simulation literature, including several cases of protein folding under confinement.

摘要

水渗透于所有生命之中,并介导着对大分子自组装过程至关重要的力。在给定的生物环境中预测这些力具有挑战性,因为水在带电和疏水面附近的组织方式不同,而这两者在体内的纳米尺度上通常都在发挥作用。在这项工作中,我们提出了一个简单的统计力学模型,用于描述不同约束表面之间水介导的力,并且证明该模型定性地统一了模拟文献中已知的广泛现象,包括几种在约束下的蛋白质折叠情况。