Department of Chemistry and Macromolecules Innovation Institute, Virginia Tech, Blacksburg, USA.
Department of Biochemistry, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada.
Curr Opin Struct Biol. 2021 Aug;69:70-77. doi: 10.1016/j.sbi.2021.03.008. Epub 2021 Apr 27.
The advent of amphiphilic copolymers enables integral membrane proteins to be solubilized into stable 10-30 nm native nanodiscs to resolve their multisubunit structures, post-translational modifications, endogenous lipid bilayers, and small molecule ligands. This breakthrough has positioned biological membrane:protein assemblies (memteins) as fundamental functional units of cellular membranes. Herein, we review copolymer design strategies and methods for the characterization of transmembrane proteins within native nanodiscs by cryo-electron microscopy (cryo-EM), transmission electron microscopy, nuclear magnetic resonance spectroscopy, electron paramagnetic resonance, X-ray diffraction, surface plasmon resonance, and mass spectrometry.
两亲性嵌段共聚物的出现使整合膜蛋白能够溶解在稳定的 10-30nm 天然纳米盘内，以解析其多亚基结构、翻译后修饰、内源性脂双层和小分子配体。这一突破将生物膜：蛋白质组装体（memteins）定位为细胞膜的基本功能单元。本文综述了通过冷冻电镜（cryo-EM）、透射电子显微镜、核磁共振波谱、电子顺磁共振、X 射线衍射、表面等离子体共振和质谱技术在天然纳米盘中对跨膜蛋白进行表征的嵌段共聚物设计策略和方法。
