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本文引用的文献

1
GROMACS 4:  Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation.GROMACS 4:高效、负载均衡和可扩展的分子模拟算法。
J Chem Theory Comput. 2008 Mar;4(3):435-47. doi: 10.1021/ct700301q.
2
P-LINCS:  A Parallel Linear Constraint Solver for Molecular Simulation.P-LINCS:一种用于分子模拟的并行线性约束求解器。
J Chem Theory Comput. 2008 Jan;4(1):116-22. doi: 10.1021/ct700200b.
3
A direct coupling between global and internal motions in a single domain protein? MD investigation of extreme scenarios.单一结构域蛋白中全局运动与内部运动的直接耦合?极端情况的 MD 研究。
Biophys J. 2011 Jul 6;101(1):196-204. doi: 10.1016/j.bpj.2011.05.041.
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Adhesive water networks facilitate binding of protein interfaces.黏附水网络促进蛋白质界面的结合。
Nat Commun. 2011 Mar 29;2:261. doi: 10.1038/ncomms1258.
5
Nuclear magnetic resonance provides a quantitative description of protein conformational flexibility on physiologically important time scales.核磁共振为蛋白质构象柔性在生理相关时间尺度上提供了定量描述。
Biochemistry. 2011 Apr 12;50(14):2735-47. doi: 10.1021/bi200177v. Epub 2011 Mar 21.
6
Site-resolved measurement of water-protein interactions by solution NMR.通过溶液 NMR 进行的基于位点的水-蛋白质相互作用测量。
Nat Struct Mol Biol. 2011 Feb;18(2):245-9. doi: 10.1038/nsmb.1955. Epub 2011 Jan 2.
7
Enhanced stability of a protein with increasing temperature.随着温度的升高,蛋白质的稳定性增强。
J Am Chem Soc. 2011 Jan 19;133(2):271-8. doi: 10.1021/ja105388k. Epub 2010 Dec 17.
8
Brownian dynamics simulation of protein solutions: structural and dynamical properties.布朗动力学模拟蛋白质溶液:结构和动力学性质。
Biophys J. 2010 Dec 1;99(11):3782-91. doi: 10.1016/j.bpj.2010.10.035.
9
Crowding and hydrodynamic interactions likely dominate in vivo macromolecular motion.拥挤和流体动力相互作用可能在体内大分子运动中起主导作用。
Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18457-62. doi: 10.1073/pnas.1011354107. Epub 2010 Oct 11.
10
The low-temperature inflection observed in neutron scattering measurements of proteins is due to methyl rotation: direct evidence using isotope labeling and molecular dynamics simulations.在蛋白质的中子散射测量中观察到的低温拐点是由于甲基旋转引起的:使用同位素标记和分子动力学模拟的直接证据。
J Am Chem Soc. 2010 Apr 14;132(14):4990-1. doi: 10.1021/ja910502g.

拥挤诱导嗜热蛋白和中温蛋白扩散的差异:对中子散射结果的新观察。

Crowding induces differences in the diffusion of thermophilic and mesophilic proteins: a new look at neutron scattering results.

机构信息

Department of Biological Chemistry and Molecular Modeling, Institute of Advanced Chemistry of Catalonia (IQAC - CSIC), Barcelona, Spain.

出版信息

Biophys J. 2011 Dec 7;101(11):2782-9. doi: 10.1016/j.bpj.2011.09.033.

DOI:10.1016/j.bpj.2011.09.033
PMID:22261067
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3297780/
Abstract

The dynamical basis underlying the increased thermal stability of thermophilic proteins remains uncertain. Here, we challenge the new paradigm established by neutron scattering experiments in solution, in which the adaptation of thermophilic proteins to high temperatures lies in the lower sensitivity of their flexibility to temperature changes. By means of a combination of molecular dynamics and Brownian dynamics simulations, we report a reinterpretation of those experiments and show evidence that under crowding conditions, such as in vivo, thermophilic and homolog mesophilic proteins have diffusional properties with different thermal behavior.

摘要

热稳定性增加的热稳定性的动力学基础仍然不确定。在这里,我们挑战了在溶液中进行的中子散射实验所建立的新范例,其中,嗜热蛋白对高温的适应在于其柔韧性对温度变化的敏感性较低。通过分子动力学和布朗动力学模拟的结合,我们重新解释了这些实验,并证明了在拥挤的条件下,如在体内,嗜热和同源嗜中温蛋白具有不同热行为的扩散性质。