Delepierre M, Dobson C M, Selvarajah S, Wedin R E, Poulsen F M
J Mol Biol. 1983 Aug 15;168(3):687-92. doi: 10.1016/s0022-2836(83)80309-x.
The solvent exchange rates of individual indole NH hydrogens of tryptophan residues of lysozyme have been measured, by using 1H 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.
利用核磁共振光谱法，在存在尿素的情况下并经过化学修饰后，测量了溶菌酶色氨酸残基中各个吲哚NH氢的溶剂交换速率与温度的函数关系。结果根据一个不依赖于蛋白质热稳定性的低活化能过程以及一个与热稳定性直接相关的较高活化能过程进行了解释。讨论了这些观察结果对理解蛋白质动力学的意义。
