Format

Send to

Choose Destination
FEBS Lett. 1998 Jun 23;430(1-2):105-11.

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

Author information

1
M.E. Müller-Institute for Microscopy, Biozentrum, University of Basel, Switzerland.

Abstract

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.

PMID:
9678604
DOI:
10.1016/s0014-5793(98)00623-1
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center