Schabert F A, Henn C, Engel A
Maurice E. Müller Institute for Microscopic Structural Biology, Universität Basel, Switzerland.
Science. 1995 Apr 7;268(5207):92-4. doi: 10.1126/science.7701347.
Topographs of two-dimensional porin OmpF crystals reconstituted in the presence of lipids were recorded in solution by atomic force microscopy (AFM) to a lateral resolution of 10 angstroms and a vertical resolution of 1 angstrom. Protein-protein interactions were demonstrated on the basis of the AFM results and earlier crystallographic findings. To assess protein-lipid interactions, the bilayer was modeled with kinked lipids by fitting the head groups to contours determined with AFM. Finally, two conformations of the extracellular porin surface were detected at forces of 0.1 nanonewton, demonstrating the potential of AFM to monitor conformational changes with high resolution.
通过原子力显微镜（AFM）在溶液中记录了在脂质存在下重构的二维孔蛋白OmpF晶体的形貌，横向分辨率为10埃，纵向分辨率为1埃。基于AFM结果和早期晶体学研究结果证明了蛋白质-蛋白质相互作用。为了评估蛋白质-脂质相互作用，通过将头部基团拟合到用AFM确定的轮廓上，用扭结脂质对双层进行建模。最后，在0.1纳牛顿的力下检测到细胞外孔蛋白表面的两种构象，证明了AFM以高分辨率监测构象变化的潜力。
