Stahlberg H, Fotiadis D, Scheuring S, Rémigy H, Braun T, Mitsuoka K, Fujiyoshi Y, Engel A
M.E.Müller-Institute for Structural Biology, University of Basel, Switzerland.
FEBS Lett. 2001 Aug 31;504(3):166-72. doi: 10.1016/s0014-5793(01)02746-6.
Electron crystallography and atomic force microscopy allow the study of two-dimensional membrane protein crystals. While electron crystallography provides atomic scale three-dimensional density maps, atomic force microscopy gives insight into the surface structure and dynamics at sub-nanometer resolution. Importantly, the membrane protein studied is in its native environment and its function can be assessed directly. The approach allows both the atomic structure of the membrane protein and the dynamics of its surface to be analyzed. In this way, the function-related conformational changes can be assessed, thus providing a detailed insight on the molecular mechanisms of essential biological processes.
电子晶体学和原子力显微镜可用于研究二维膜蛋白晶体。电子晶体学能够提供原子尺度的三维密度图,而原子力显微镜则能在亚纳米分辨率下洞察表面结构和动力学。重要的是,所研究的膜蛋白处于其天然环境中,其功能可直接进行评估。该方法既能分析膜蛋白的原子结构,又能分析其表面动力学。通过这种方式,可以评估与功能相关的构象变化,从而深入了解基本生物学过程的分子机制。