ELECTROSTATIC EFFECTS AND HYDROGEN-EXCHANGE BEHAVIOR IN PROTEINS - THE PH-DEPENDENCE OF EXCHANGE-RATES IN LYSOZYME
ELECTROSTATIC EFFECTS AND HYDROGEN-EXCHANGE BEHAVIOR IN PROTEINS - THE PH-DEPENDENCE OF EXCHANGE-RATES IN LYSOZYME
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DOI：
10.1016/0022-2836(87)90613-9
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发表时间：
1987-09-05
影响因子：
5.6
通讯作者：
WEDIN, RE
中科院分区：
文献类型：
--
作者：
DELEPIERRE, M;DOBSON, CM;WEDIN, RE
在低于热变性温度的温度下，测定了鸡蛋清溶菌酶中色氨酸和酰胺氢原子的交换速率对pH值的依赖性。每种氢的pH值行为都是独特的，并且可以与简单化合物的pH值行为显著不同。蛋白质中的静电效应的一个模型被描述和用来解释一些功能的pH值依赖的某些氢的交换率。结果表明，交换发生从蛋白质的构象非常相似的天然蛋白质，与本地波动提供的交换机制。对于更多的埋在低pH值的氢有一个普遍增加的交换率所造成的蛋白质的稳定性下降，从静电模型计算。分析表明，氢交换研究的证据可以用来提供有关蛋白质局部区域静电相互作用的信息。静电模型的描述和一些应用在附录中给出。
The pH dependence of the exchange rates for a number of tryptophan and amide hydrogen atoms in hen egg-white lysozyme has been determined at temperatures well below the thermal denaturation temperature. The pH behaviour of each hydrogen is unique and can differ markedly from that of simple compounds. A model for electrostatic effects in proteins is described and used to explain a number of the features of the pH dependence of the exchange rates of certain hydrogens. The results indicate that exchange takes place from a conformation of the protein closely similar to that of the native protein, with local fluctuations providing the mechanism for exchange. For the more-buried hydrogens at low pH values there is a general increase in the exchange rates caused by the decreasing stability of the protein as calculated from the electrostatic model. The analysis shows how evidence from hydrogen exchange studies can be used to provide information about electrostatic interactions in localized regions of proteins. A description of the electrostatic model and some applications are given in the Appendix.