Correlation of hydrogen exchange behaviour and thermal stability of lysozyme.
Correlation of hydrogen exchange behaviour and thermal stability of lysozyme.
复制标题
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
复制
发表时间:
1983
影响因子:
5.6
通讯作者:
F. Poulsen
中科院分区:
文献类型:
--
作者:
M. Delepierre;C. Dobson;S. Selvarajah;R. Wedin;F. Poulsen
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.
影响因子:
2.9
作者:
Wedin,RE;Delepierre,M;Dobson,CM;Poulsen,FM
通讯作者:
Poulsen,FM