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首页> 外文期刊>Journal of Molecular Biology >Determination of intramolecular distance distribution during protein folding on the millisecond timescale.
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Determination of intramolecular distance distribution during protein folding on the millisecond timescale.

机译：在毫秒时间尺度上确定蛋白质折叠过程中的分子内距离分布。

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摘要

A method for determination of transient (on the millisecond timescale) intramolecular distance distributions (IDDs) by time-resolved dynamic non-radiative excitation energy transfer measurements was developed. The time-course of the development of the IDD between residues 73 and 203 in the CORE domain of Escherichia coli adenylate kinase throughout refolding from the GuHCl-induced denatured state was determined. The mean of the apparent IDD reduced to a value close to its magnitude in the native protein, within 2 ms (the dead-time of the instrument). At that time the width of that distribution was rather large (16+/-2 A). The large width implies that the intramolecular diffusion coefficient of the labeled segment does not exceed 10(-7) cm(2)/second. In a second slower phase of the refolding transition, the width was reduced to its native value (6+/-4 A). Copyright 2000 Academic Press.
机译：开发了一种通过时间分辨动态非辐射激发能转移测量来确定瞬态（毫秒级）分子内距离分布（IDD）的方法。确定了在从GuHCl诱导的变性状态重新折叠的整个过程中，大肠杆菌腺苷酸激酶CORE结构域中残基73和203之间IDD发展的时程。表观IDD的平均值在2毫秒（仪器的死区时间）之内减小到接近其在天然蛋白质中的大小的值。那时该分布的宽度相当大（16 +/- 2 A）。大宽度意味着标记段的分子内扩散系数不超过10（-7）cm（2）/秒。在重新折叠过渡的第二个较慢阶段，宽度减小到其原始值（6 +/- 4 A）。版权所有2000学术出版社。

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