Dynamics of spin-labelled α-chymotrypsin in reverse micelles of differently charged surfactants
Dynamics of spin-labelled α-chymotrypsin in reverse micelles of differently charged surfactants
复制标题
自旋标记的α-胰凝乳蛋白酶在不同电荷表面活性剂反胶束中的动力学
DOI：
10.1039/ft9969203151
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
B. C. Gilbert
中科院分区：
文献类型：
--
作者：
H. Căldăraru;G. Timmins;M. Davies;B. C. Gilbert
对α-糜蛋白酶在水和二（2-乙基己基）磺基琥珀酸钠（AOT）-异辛烷反胶团中两个位点（蛋氨酸-192和丝氨酸-195）自旋标记的EPR谱进行了分析和模拟，提供了标记物在这些介质中运动的速率和性质的信息。甲硫氨酸标记的胰凝乳蛋白酶的相关时间，和丝氨酸标记的胰凝乳蛋白酶在反胶束中的A的值已被研究作为功能的表面活性剂电荷[AOT，负，和十六烷基三甲基溴化铵（CTAB），正]，净蛋白质的电荷以上和以下的等电点，并添加中性辅助表面活性剂。所获得的结果是一致的“水壳”模型的蛋白质溶剂化在这些系统中，没有证据表明蛋白质和表面活性剂头基之间的任何离子显着的相互作用。
Analysis and simulation of the EPR spectra of α-chymotrypsin spin-labelled at two sites (methionine-192 and serine-195) in water and sodium bis(2-ethylhexyl) sulfosuccinate (AOT)–isooctane reverse micelles has provided information on the rate and nature of label motion in these media. The correlation time of methionine-labelled chymotrypsin, and the value of A∥ for serine-labelled chymotrypsin in reverse micelles have been studied as functions of surfactant charge [AOT, negative, and cetyltrimethylammonium bromide (CTAB), positive], of the net protein charge above and below its isoelectric point, and of the addition of neutral co-surfactants. The results obtained are consistent with the ‘water-shell’ model of protein solvation in these systems, with no evidence for any ionic significant interactions between protein and surfactant headgroups.