TC Jenkins Department of Biophysics, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD, 21218, United States.
TC Jenkins Department of Biophysics, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD, 21218, United States.
Curr Opin Struct Biol. 2021 Aug;69:124-130. doi: 10.1016/j.sbi.2021.03.006. Epub 2021 May 8.
Membrane proteins have historically been recalcitrant to biophysical folding studies. However, recent adaptations of methods from the soluble protein folding field have found success in their applications to transmembrane proteins composed of both α-helical and β-barrel conformations. Avoiding aggregation is critical for the success of these experiments. Altogether these studies are leading to discoveries of folding trajectories, foundational stabilizing forces and better-defined endpoints that enable more accurate interpretation of thermodynamic data. Increased information on membrane protein folding in the cell shows that the emerging biophysical principles are largely recapitulated even in the complex biological environment.
膜蛋白的生物物理折叠研究一直以来都很困难。然而，可溶性蛋白折叠领域方法的最新改进在应用于由α-螺旋和β-桶构象组成的跨膜蛋白时取得了成功。避免聚集对于这些实验的成功至关重要。总的来说，这些研究正在揭示折叠轨迹、基础稳定力和更明确的终点，从而能够更准确地解释热力学数据。关于细胞中膜蛋白折叠的信息不断增加，表明即使在复杂的生物环境中，新兴的生物物理原理也在很大程度上得到了再现。
