Müller D J, Fotiadis D, Engel A
M.E. Müller-Institute for Microscopy, Biozentrum, University of Basel, Switzerland.
FEBS Lett. 1998 Jun 23;430(1-2):105-11. doi: 10.1016/s0014-5793(98)00623-1.
The mapping of flexible protein domains with the atomic force microscope is reviewed. Examples discussed are the bacteriorhodopsin from Halobacterium salinarum, the head-tail-connector from phage phi29, and the hexagonally packed intermediate layer from Deinococcus radiodurans which all were recorded in physiological buffer solution. All three proteins undergo reversible structural changes that are reflected in standard deviation maps calculated from aligned topographs of individual protein complexes. Depending on the lateral resolution (up to 0.8 nm) flexible surface regions can ultimately be correlated with individual polypeptide loops. In addition, multivariate statistical classification revealed the major conformations of the protein surface.
本文综述了利用原子力显微镜对柔性蛋白质结构域的成像研究。讨论的例子包括盐生盐杆菌的细菌视紫红质、噬菌体φ29的头尾连接体以及耐辐射球菌的六角形堆积中间层，这些都是在生理缓冲溶液中记录的。所有这三种蛋白质都经历了可逆的结构变化，这在从单个蛋白质复合物的对齐形貌图计算出的标准差图中得到了体现。根据横向分辨率（高达0.8纳米），最终可以将柔性表面区域与单个多肽环相关联。此外，多变量统计分类揭示了蛋白质表面的主要构象。
