Sampling the conformational space of membrane protein surfaces with the AFM

被引:55
作者
Scheuring, S
Müller, DJ
Stahlberg, H
Engel, HA
Engel, A
机构
[1] Univ Basel, Biozentrum, ME Muller Inst Microscopy, CH-4056 Basel, Switzerland
[2] Max Planck Inst Mol Cell Biol & Genet, D-01307 Dresden, Germany
[3] Univ Basel, Dept Phys & Astron, CH-4056 Basel, Switzerland
来源
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2002年 / 31卷 / 03期
关键词
loops; beta-turns; membrane protein; two-dimensional crystal; energy landscape;
D O I
10.1007/s00249-001-0197-8
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
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 OrnpF, aquaporin-Z, and bacteriorhodopsin, all recorded at a lateral resolution of <7 &ANGS; and a vertical resolution of ∼1 &ANGS;. 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.
引用
收藏
页码:172 / 178
页数:7
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