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通过质子核磁共振研究溶菌酶与水的相互作用性质

Nature of lysozyme-water interactions by proton NMR.

作者信息

Prosser S, Peemoeller H

机构信息

Department of Physics, University of Waterloo, Ont., Canada.

出版信息

Biochem Cell Biol. 1991 May-Jun;69(5-6):341-5.

PMID:1654941
Abstract

Proton spin-lattice relaxation measurements were performed in 10 mM lysozyme solution as a function of temperature and degree of substitution of solvent H2O with D2O. The results show that in the temperature range from 274 to 323 K, the intermolecular lysozyme proton water proton coupling contributes appreciably to the observed water proton relaxation rate. In this system exchange between water protons and labile protein protons does not dominate the behaviour with temperature of the water-lysozyme intermolecular contribution to the spin-lattice relaxation.

摘要

在10 mM溶菌酶溶液中进行了质子自旋晶格弛豫测量,测量结果是温度和溶剂H2O被D2O取代程度的函数。结果表明,在274至323 K的温度范围内,分子间溶菌酶质子与水质子的耦合对观测到的水质子弛豫率有显著贡献。在该体系中,水质子与不稳定蛋白质质子之间的交换对水-溶菌酶分子间自旋晶格弛豫贡献随温度的变化行为不起主导作用。

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