CERM, and Department of Chemistry U. Schiff, University of Florence, Sesto Fiorentino, Italy.
J Phys Chem B. 2013 Apr 4;117(13):3548-53. doi: 10.1021/jp312561f. Epub 2013 Mar 25.
Reorientation correlation times in protein solutions are key determinants for feasibility and quality of NMR experiments. Yet, their accurate estimate is not easy, especially in the case of very large proteins. We show that nuclear magnetic relaxation dispersion (NMRD) can accurately determine reorientation times up to the microsecond range. A theoretical description for the analysis of the NMRD profiles is provided, and the protein reorientation time is shown to be provided by the longest correlation time among those needed to reproduce the experimental profile. Measurements are performed using samples of the archaeal proteasome double ring α7α7 and of αB-Crystallin in glycerol solutions.
在蛋白质溶液中，重新取向相关时间是决定 NMR 实验可行性和质量的关键因素。然而，要准确估计这些时间并不容易，尤其是在非常大的蛋白质的情况下。我们表明，核磁共振弛豫分散（NMRD）可以精确地确定重新取向时间，直至微秒范围。提供了一种用于分析 NMRD 谱图的理论描述，并表明蛋白质的重新取向时间是通过复制实验谱图所需的最长相关时间来提供的。使用古细菌蛋白酶体双环α7α7 和甘油溶液中的αB-晶体蛋白的样品进行测量。
