Bacteriorhodopsin.

J K Lanyi, H Luecke

Journal: Current opinion in structural biology 2001;11(4):415-9

PMID: 11495732

Full Text on Elsevier Science View on PubMed

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.

Address: Department of Physiology and Biophysics, University of California, Irvine, CA 92697, USA. [email protected]

DOI: 10.1016/s0959-440x(00)00226-8

Link outs

Subscription / membership required

Full Text Sources:

https://linkinghub.elsevier.com/retrieve/pii/S0959...

MeSH Terms: Bacteriorhodopsins, Ion Transport, Isomerism, Light, Membrane Proteins, Models, Structural, Protein Conformation, Proton Pumps, Purple Membrane, Retinaldehyde, Water, X-Ray Diffraction