Hydrogen exchange and the dynamic structure of proteins
Hydrogen exchange and the dynamic structure of proteins
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DOI：
10.1007/bf00421225
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发表时间：
1982-10
影响因子：
4.3
通讯作者：
C. Woodward;I. Simon;E. Tüchsen
中科院分区：
文献类型：
--
作者：
C. Woodward;I. Simon;E. Tüchsen
在天然蛋白质中，埋藏的不稳定质子与溶剂氢进行同位素交换，但交换动力学明显慢于未折叠的多肽。这表明，虽然被掩埋的蛋白质原子不受溶剂的影响，但蛋白质在时间平均结构周围波动，偶尔会将被掩埋的部位暴露在溶剂中。一般来说，氢交换研究的目的是表征构象亚态之间波动的性质，监测由于配体结合或其他因素导致的蛋白质亚态之间构象平衡的变化，或监测主要的协同变性转变。本文综述了蛋白质中氢交换的最新报道，重点介绍了方法上的最新进展，特别是研究结果对折叠蛋白质中氢交换机制的影响。
In native proteins, buried, labile protons undergo isotope exchange with solvent hydrogens, but the kinetics of exchange are markedly slower than in unfolded polypeptides. This indicates that, whereas buried protein atoms are shielded from solvent, the protein fluctuates around the time average structure and occasionally exposes buried sites to solvent. Generally, hydrogen exchange studies are designed to characterize the nature of the fluctuations between conformational substates, to monitor the shift in conformational equilibria among protein substates due to ligand binding or other factors, or to monitor the major cooperative denaturation transition. In this article, we review the recent reports of hydrogen exchange in proteins, focusing on recent advances in methodology, especially with regard to the implications of the results for the mechanism of hydrogen exchange in folded proteins.