Characterisation of protein unfolding by NMR diffusion measurements
Characterisation of protein unfolding by NMR diffusion measurements
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DOI：
10.1023/a:1018304117895
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发表时间：
1997-09-01
影响因子：
2.7
通讯作者：
Dobson, CM
中科院分区：
文献类型：
--
作者：
Jones, JA;Wilkins, DK;Dobson, CM
蛋白质非天然状态的表征是蛋白质折叠研究中的一个关键问题。这些状态的完整表征需要描述局部和全局性质，包括分子尺寸。在这里，我们提出了脉冲场梯度实验的结果，旨在比较在本地和非本地状态的蛋白质的有效流体动力学半径。对溶菌酶进行的测量表明，在尿素中展开时，有效流体动力学半径增加了38+/-1%，这一结果与最近通过小角X射线散射进行的研究完全一致。
The characterisation of non-native stales of proteins is a key problem in studies of protein folding. Complete characterisation of these states requires a description of both local and global properties, including molecular dimensions. Here we present results from pulsed field gradient experiments designed to compare the effective hydrodynamic radii of a protein in native and non-native states. Measurements performed on lysozyme indicate that the effective hydrodynamic radius increases by 38+/-1% on unfolding in urea, a result completely consistent with a recent study by small-angle X-ray scattering.