Department of Physics and Optical Sciences, University of North Carolina, Charlotte, NC, United States; Center for Biomedical Engineering and Science, University of North Carolina, Charlotte, NC, United States.
Department of Physics, Kazan Federal University, Kazan, Russia.
Prog Mol Biol Transl Sci. 2019;166:85-108. doi: 10.1016/bs.pmbts.2019.05.004. Epub 2019 Jun 8.
Translational (or self-diffusion) coefficient in dilute solution is inversely proportional to the size of a diffusing molecule, and hence self-diffusion coefficient measurements have been applied to determine the effective hydrodynamic radii for a range of native and nonnative protein conformations. In particular, translational diffusion coefficient measurements are useful to estimate the hydrodynamic radius of natively (or intrinsically) disordered proteins in solution, and, thereby, probe the compactness of a protein as well as its change when environmental parameters such as temperature, solution pH, or protein concentration are varied. The situation becomes more complicated in concentrated solutions. In this review, we discuss the translational diffusion of disordered proteins in dilute and crowded solutions, focusing primarily on the information provided by pulsed-field gradient NMR technique, and draw analogies to well-structured globular proteins and synthetic polymers.
在稀溶液中，扩散分子的尺寸与平移（或自扩散）系数成反比，因此自扩散系数的测量已被应用于确定一系列天然和非天然蛋白质构象的有效流体力学半径。特别是，平移扩散系数的测量有助于估计溶液中天然（或固有）无规卷曲蛋白质的流体力学半径，从而可以探测蛋白质的紧凑性及其在环境参数（如温度、溶液 pH 值或蛋白质浓度）变化时的变化。在高浓度溶液中，情况变得更加复杂。在这篇综述中，我们讨论了无序蛋白质在稀溶液和拥挤溶液中的平移扩散，主要关注脉冲梯度 NMR 技术提供的信息，并与结构良好的球状蛋白质和合成聚合物进行类比。
