Format

Send to

Choose Destination
J Mol Biol. 1999 Feb 5;285(5):1903-9.

Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane.

Author information

1
M. E. Müller-Institute for Microscopic Structural Biology, Biozentrum University of Basel, Klingelbergstrasse 70, Basel, CH-4056, Switzerland. muellerda@ubaclu.unibas.ch

Abstract

Bacteriorhodopsin is the one of the best-studied models of an ion pump. Five atomic models are now available, yet their comparison reveals differences of some loops connecting the seven transmembrane alpha-helices. In an attempt to resolve this enigma, topographs were recorded in aqueous solution with the atomic force microscope (AFM) to reveal the most native surface structure of bacteriorhodopsin molecules in the purple membrane. Individual peptide loops were observed with a lateral resolution of between 4.5 A and 5.8 A, and a vertical resolution of about 1 A. The AFM images demonstrate for the first time, that the shape, the position, and the flexibility of individual polypeptide loops depend on the packing arrangement of bacteriorhodopsin molecules in the lipid bilayer.

PMID:
9925773
DOI:
10.1006/jmbi.1998.2441
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center