Journal Article

PreJuSER-38377

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The molecular mechanism of membrane proteins probed by evanescent infrared waves

Nyquist, R. M. ; Ataka, K.FZJ* ; Heberle, J.FZJ*

2004
Wiley-VCH Weinheim

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Please use a persistent id in citations: doi:10.1002/cbic.200300687

Abstract: The catalytic action of membrane proteins is vital to many cellular processes. Yet the molecular mechanisms remain poorly understood. We describe here the technique of evanescent infrared difference spectroscopy as a tool to decipher the structural changes associated with the enzymatic action of membrane proteins. Functional changes as minute as the protonation state of individual amino acid side chains can be observed and linked to interactions with a ligand, agonist, effector, or redox partner.

Keyword(s): Bacteriorhodopsins: chemistry (MeSH) ; Bacteriorhodopsins: metabolism (MeSH) ; Electron Transport Complex IV: chemistry (MeSH) ; Electron Transport Complex IV: metabolism (MeSH) ; Membrane Proteins: chemistry (MeSH) ; Membrane Proteins: metabolism (MeSH) ; Rhodopsin: chemistry (MeSH) ; Rhodopsin: metabolism (MeSH) ; Spectrophotometry, Infrared: methods (MeSH) ; Membrane Proteins ; Bacteriorhodopsins ; Rhodopsin ; Electron Transport Complex IV ; J ; attenuated total reflection spectroscopy (auto) ; bacteriorhodopsin (auto) ; cytochrome c oxidase (auto) ; IR spectroscopy (auto) ; membrane proteins (auto) ; reaction mechanisms (auto)

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Biologische Strukturforschung (IBI-2)

Research Program(s):

1. Neurowissenschaften (L01)

Appears in the scientific report 2004

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