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本文引用的文献

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Fingerprints of amorphous icelike behavior in the vibrational density of states of protein hydration water.蛋白质水化水中态密度的非晶态冰状行为指纹图谱。
Phys Rev Lett. 2008 Oct 3;101(14):148104. doi: 10.1103/PhysRevLett.101.148104.
2
Coincidence of dynamical transitions in a soluble protein and its hydration water: direct measurements by neutron scattering and MD simulations.可溶性蛋白质及其水化水动力学转变的巧合:通过中子散射和分子动力学模拟进行直接测量。
J Am Chem Soc. 2008 Apr 9;130(14):4586-7. doi: 10.1021/ja710526r. Epub 2008 Mar 14.
3
The dynamical transition of proteins, concepts and misconceptions.蛋白质的动态转变:概念与误解
Eur Biophys J. 2008 Jun;37(5):591-602. doi: 10.1007/s00249-008-0274-3. Epub 2008 Feb 13.
4
Preservation of membranes in anhydrobiotic organisms: the role of trehalose.脱水生物体内膜的保存:海藻糖的作用。
Science. 1984 Feb 17;223(4637):701-3. doi: 10.1126/science.223.4637.701.
5
The dynamic susceptibility in glass forming molecular liquids: the search for universal relaxation patterns II.玻璃形成分子液体中的动态磁化率:通用弛豫模式的探寻II。
J Chem Phys. 2006 Apr 7;124(13):134503. doi: 10.1063/1.2178316.
6
Macro- and microdefinitions of fragility of hydrogen-bonded glass-forming liquids.
Phys Rev E Stat Nonlin Soft Matter Phys. 2006 Mar;73(3 Pt 1):031201. doi: 10.1103/PhysRevE.73.031201. Epub 2006 Mar 23.
7
Coupling between lysozyme and trehalose dynamics: microscopic insights from molecular-dynamics simulations.溶菌酶与海藻糖动力学之间的耦合:分子动力学模拟的微观见解
J Chem Phys. 2006 Jan 21;124(3):034901. doi: 10.1063/1.2159471.
8
Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glasses, control protein motions and functions.大量溶剂和水化层波动,类似于玻璃中的α和β波动,控制着蛋白质的运动和功能。
Proc Natl Acad Sci U S A. 2004 Oct 5;101(40):14408-13. doi: 10.1073/pnas.0405573101. Epub 2004 Sep 24.
9
Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase.对dUTP酶催化磷酸酯水解机制的结构洞察。
J Biol Chem. 2004 Oct 8;279(41):42907-15. doi: 10.1074/jbc.M406135200. Epub 2004 Jun 17.
10
Mean-square displacement relationship in bioprotectant systems by elastic neutron scattering.通过弹性中子散射研究生物保护剂系统中的均方位移关系。
Biophys J. 2004 May;86(5):3241-9. doi: 10.1016/S0006-3495(04)74372-6.

通过中子散射研究溶剂 - 蛋白质耦合效应。

Study of solvent-protein coupling effects by neutron scattering.

作者信息

Varga B, Migliardo F, Takacs E, Vertessy B, Magazù Salvatore, Telling M T F

出版信息

J Biol Phys. 2010 Mar;36(2):207-20. doi: 10.1007/s10867-009-9177-5. Epub 2009 Oct 1.

DOI:10.1007/s10867-009-9177-5
PMID:19795216
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2825304/
Abstract

The present work aims to characterize the dynamical behavior of proteins immersed in bio-preserving liquids and glasses. For this purpose, the protein dUTPase was chosen, while the selected solvents were glycerol, a triol, and some homologous disaccharides, i.e., trehalose, maltose, and sucrose, which are known to be very effective bio-preserving agents. The results highlight that the disaccharides show a slowing down effect on the water dynamics, which is stronger for trehalose than in the case of the other disaccharides. Furthermore, a characterization of the medium which hosts the protein is performed by using an operative definition of fragility based on the mean square displacement extracted by elastic incoherent neutron scattering, which is directly connected to Angell's kinetic fragility based on the viscosity. Finally, a study of the dynamics of the protein sequestered within the solvents is performed. The result shows that the protein dynamics is coupled with that of the surrounding matrix.

摘要

本研究旨在表征浸入生物保存液和玻璃中的蛋白质的动力学行为。为此,选择了蛋白质dUTPase,而选定的溶剂是甘油(一种三元醇)和一些同源二糖,即海藻糖、麦芽糖和蔗糖,它们已知是非常有效的生物保存剂。结果表明,二糖对水动力学有减缓作用,海藻糖的这种作用比其他二糖更强。此外,通过基于弹性非相干中子散射提取的均方位移对脆性进行操作定义,来对容纳蛋白质的介质进行表征,该均方位移与基于粘度的安吉尔动力学脆性直接相关。最后,对溶剂中隔离的蛋白质的动力学进行了研究。结果表明,蛋白质动力学与周围基质的动力学相互耦合。