Correlation of hydrogen exchange behaviour and thermal stability of lysozyme.

Correlation of hydrogen exchange behaviour and thermal stability of lysozyme.
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溶菌酶氢交换行为与热稳定性的相关性。

DOI:
10.1016/s0022-2836(83)80309-x
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发表时间:
1983
影响因子:
5.6
通讯作者:
F. Poulsen
F. Poulsen
中科院分区:
生物学2区
文献类型:
--
作者:
M. Delepierre;C. Dobson;S. Selvarajah;R. Wedin;F. Poulsen

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本文用~ 1H核磁共振法测定了溶菌酶色氨酸残基上吲哚NH氢的溶剂交换速率随温度的变化。结果已被解释在一个低活化能的过程,这是不依赖于蛋白质的热稳定性,和一个较高的活化能的过程,这是直接与热稳定性。这些意见的蛋白质的动力学的理解的意义进行了讨论。
The solvent exchange rates of individual indole NH hydrogens of tryptophan residues of lysozyme have been measured, by using1H nuclear magnetic resonance spectroscopy, as a function of temperature in the presence of urea and following chemical modification. The results have been interpreted in terms of a low activation energy process which is not dependent on the thermal stability of the protein, and a higher activation energy process that is directly correlated with the thermal stability. The significance of these observations for an understanding of the dynamics of the protein is discussed.
DOI: 10.1021/bi00534a042
发表时间: 1982
期刊: Biochemistry
影响因子: 2.9
作者:
Wedin,RE;Delepierre,M;Dobson,CM;Poulsen,FM
通讯作者: Poulsen,FM