DETECTION OF TRANSIENT PROTEIN-FOLDING POPULATIONS BY MASS-SPECTROMETRY
DETECTION OF TRANSIENT PROTEIN-FOLDING POPULATIONS BY MASS-SPECTROMETRY
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DOI：
10.1126/science.8235611
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发表时间：
1993-11-05
期刊：
影响因子：
56.9
通讯作者：
DOBSON, CM
中科院分区：
文献类型：
--
作者：
MIRANKER, A;ROBINSON, CV;DOBSON, CM
氢-氘交换测量在蛋白质分子动力学研究中变得越来越重要，特别是在蛋白质分子折叠行为研究中。电喷雾电离质谱法（ESI-MS）已被用于获得在溶液中发生氢交换的蛋白质分子群内的质量分布。这一信息与核磁共振波谱（NMR）实验的结果是互补的，核磁共振波谱测量的是蛋白质分子分布中单个位点的平均占用率。在母鸡溶菌酶的实验中，采用ESI-MS和NMR相结合的方法来区分氢交换的不同机制，从而深入了解瞬时折叠中间体的性质和种群。这些结果有助于详细描述蛋白质在再折叠过程中可用的途径。
Hydrogen-deuterium exchange measurements are becoming increasingly important in studies of the dynamics of protein molecules and, particularly, of their folding behavior. Electrospray ionization mass spectrometry (ESI-MS) has been used to obtain the distribution of masses within a population of protein molecules that had undergone hydrogen exchange in solution. This information is complementary to that from nuclear magnetic resonance spectroscopy (NMR) experiments, which measure the average occupancy of individual sites over the distribution of protein molecules. In experiments with hen lysozyme, a combination of ESI-MS and NMR was used to distinguish between alternative mechanisms of hydrogen exchange, providing insight into the nature and populations of transient folding intermediates. These results have helped to detail the pathways available to a protein during refolding.