Mapping flexible protein domains at subnanometer resolution with the atomic force microscope

FEBS Letters

Müller, Daniel J¹  Fotiadis, Dimitrios¹  Engel, Andreas¹ 

[1] M.E. Müller-Institute for Microscopy, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland

关键词: Atomic force microscopy;    Hexagonally packed intermediate layer;    Phage φ29 head-to-tail connector;    Protein flexibility;    Purple membrane;    AFM;    atomic force microscopy;    HPI layer;    hexagonally packed intermediate layer;    RMS;    root-mean-square;    SD;    standard deviation;    S/N;    signal-to-noise;   

DOI  :  10.1016/S0014-5793(98)00623-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 φ29, 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.

【 授权许可】

Unknown