Scheuring Simon, Müller Daniel J, Stahlberg Henning, Engel Hans-Andreas, Engel Andreas
M.E. Müller Institute for Microscopy at the Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland.
Eur Biophys J. 2002 Jun;31(3):172-8. doi: 10.1007/s00249-001-0197-8. Epub 2002 Jan 29.
The atomic force microscope acquires topographs of single native membrane proteins at subnanometer resolution. Owing to the high signal-to-noise ratio, such images allow the conformational space of membrane protein surfaces to be sampled. This is demonstrated by topographs of porin OmpF, aquaporin-Z, and bacteriorhodopsin, all recorded at a lateral resolution of <7 A and a vertical resolution of ~1 A. The amplitudes of the domain movements were estimated from a large number of single molecule topographs and the corresponding energy landscapes calculated. To visualize the motion of protein domains, movies were generated by similarity ranking of the observed protein configurations. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00249-001-0197-8
原子力显微镜以亚纳米分辨率获取单个天然膜蛋白的拓扑图。由于信噪比高，此类图像能够对膜蛋白表面的构象空间进行采样。孔蛋白OmpF、水通道蛋白Z和细菌视紫红质的拓扑图均证明了这一点，所有这些拓扑图的横向分辨率均<7 Å，纵向分辨率约为1 Å。通过大量单分子拓扑图估计结构域运动的幅度，并计算相应的能量景观。为了可视化蛋白质结构域的运动，通过对观察到的蛋白质构型进行相似性排序生成了电影。本文的电子补充材料可通过位于http://dx.doi.org/10.1007/s00249-001-0197-8的Springer Link服务器获取
