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首页> 外文期刊>Journal of Molecular Biology >Microsecond to minute dynamics revealed by EX1-type hydrogen exchange at nearly every backbone hydrogen bond in a native protein.
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Microsecond to minute dynamics revealed by EX1-type hydrogen exchange at nearly every backbone hydrogen bond in a native protein.

机译：在天然蛋白质的几乎每个主链氢键处，EX1型氢交换揭示了微秒到分钟的动力学。

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摘要

A previous comprehensive analysis of the pH dependence of native-state amide hydrogen (NH) exchange in turkey ovomucoid third domain (OMTKY3) yielded apparent opening and closing rate constants (k(op) and k(cl)) at 14 NH groups involved in global conformational changes. This analysis has been extended to 18 additional slowly exchanging NH groups. Quench-flow experiments were performed to monitor NH exchange in native OMTKY3 from neutral to very alkaline pH ( approximately 12) conditions. Above pH 10 the mechanism of exchange switched from one governed by a rapid equilibrium preceding the chemistry of exchange (i.e. EX2 exchange), to one where exchange was limited by the rate of opening (i.e. EX1 exchange). Kinetics of solvent exposure are now known for nearly all backbone NH groups in native OMTKY3, yielding rate constants that span five orders of magnitude, 0.004 to 200 s(-1). Copyright 2000 Academic Press.
机译：先前对土耳其卵类粘液第三域（OMTKY3）中天然酰胺氢（NH）交换的pH依赖性的综合分析得出了涉及14个NH基团的表观打开和闭合速率常数（k（op）和k（cl））。全球构象变化。该分析已扩展至另外18个缓慢交换的NH基团。进行猝灭流动实验以监测天然OMTKY3中从中性到非常碱性的pH（大约12）条件下的NH交换。在pH高于10时，交换机制从一种由交换化学之前的快速平衡控制的机制（即EX2交换）切换到一种交换受开放速率限制的机制（即EX1交换）。现在已知天然OMTKY3中几乎所有主链NH基团的溶剂暴露动力学，其速率常数跨越5个数量级，0.004至200 s（-1）。版权所有2000学术出版社。

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