Force-induced conformational change of bacteriorhodopsin.

Abstract:

:The cytoplasmic surface topography of purple membranes imaged by the atomic force microscope depends mainly on the force applied to the stylus. Imaged at forces of 300 pN, individual bacteriorhodopsin molecules reveal two domains. The resulting donut-shaped trimers reversibly transform into structures exhibiting three prominent protrusions when scanned at 100 pN. In parallel, the height of the protein moiety above the lipid layer increases from 4 A to 6 A. From the known structure of bacteriorhodopsin it appears that this change may be related to a bending of the most prominent cytoplasmic loop.

journal_name

J Mol Biol

authors

Müller DJ,Büldt G,Engel A

doi

10.1006/jmbi.1995.0292

subject

Has Abstract

pub_date

1995-06-02 00:00:00

pages

239-43

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(85)70292-6

journal_volume

249

pub_type

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