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@ARTICLE{Nyquist:38377,
author = {Nyquist, R. M. and Ataka, K. and Heberle, J.},
title = {{T}he molecular mechanism of membrane proteins probed by
evanescent infrared waves},
journal = {ChemBioChem},
volume = {5},
issn = {1439-4227},
address = {Weinheim},
publisher = {Wiley-VCH},
reportid = {PreJuSER-38377},
pages = {431 - 436},
year = {2004},
note = {Record converted from VDB: 12.11.2012},
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.},
keywords = {Bacteriorhodopsins: chemistry / Bacteriorhodopsins:
metabolism / Electron Transport Complex IV: chemistry /
Electron Transport Complex IV: metabolism / Membrane
Proteins: chemistry / Membrane Proteins: metabolism /
Rhodopsin: chemistry / Rhodopsin: metabolism /
Spectrophotometry, Infrared: methods / Membrane Proteins
(NLM Chemicals) / Bacteriorhodopsins (NLM Chemicals) /
Rhodopsin (NLM Chemicals) / Electron Transport Complex IV
(NLM Chemicals) / J (WoSType)},
cin = {IBI-2},
ddc = {540},
cid = {I:(DE-Juel1)VDB58},
pnm = {Neurowissenschaften},
pid = {G:(DE-Juel1)FUEK255},
shelfmark = {Biochemistry $\&$ Molecular Biology / Chemistry, Medicinal},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:15185365},
UT = {WOS:000220773500004},
doi = {10.1002/cbic.200300687},
url = {https://juser.fz-juelich.de/record/38377},
}