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Curr Opin Struct Biol. 2001 Aug;11(4):415-9.

Bacteriorhodopsin.

Author information

1
Department of Physiology and Biophysics, University of California, Irvine, CA 92697, USA. jlanyi@orion.uci.edu

Abstract

High-resolution maps from X-ray diffraction of bacteriorhodopsin and some of its photointermediates have yielded insights into how the isomerization of the bound retinal drives ion transport. Although important mechanistic details are still undecided, the events of the photochemical cycle are now understood to reflect changes in specific hydrogen bonds of protein groups and bound water molecules in response to motions of the retinal chain.

PMID:
11495732
DOI:
10.1016/s0959-440x(00)00226-8
[Indexed for MEDLINE]

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