Tillett M L, Horsfield M A, Lian L Y, Norwood T J
Biological NMR Centre, Leicester University, U.K.
J Biomol NMR. 1999 Mar;13(3):223-32. doi: 10.1023/a:1008301324954.
NMR diffusion coefficient measurements have been shown to be sensitive to the conformational and oligomeric states of proteins. Recently, heteronuclear-filtered diffusion experiments have been proposed [Dingley et al. (1997) J. Biomol. NMR, 10, 1-8]. Several new heteronuclear-filtered diffusion pulse sequences are proposed which are shown to have superior sensitivity to those previously proposed. One of these new heteronuclear-filtered diffusion experiments has been used to study the binding of an SH3 domain to a peptide. Using this system, we show that it is possible to measure binding constants from diffusion coefficient measurements.
核磁共振扩散系数测量已被证明对蛋白质的构象和寡聚状态敏感。最近，有人提出了异核过滤扩散实验[丁利等人（1997年）《生物分子核磁共振杂志》，10，1 - 8]。本文提出了几种新的异核过滤扩散脉冲序列，结果表明它们比先前提出的序列具有更高的灵敏度。其中一种新的异核过滤扩散实验已被用于研究SH3结构域与一种肽的结合。利用这个系统，我们表明可以从扩散系数测量中测定结合常数。
