TY  - JOUR
AU  - Nyquist, R. M.
AU  - Ataka, K.
AU  - Heberle, J.
TI  - The molecular mechanism of membrane proteins probed by evanescent infrared waves
JO  - ChemBioChem
VL  - 5
SN  - 1439-4227
CY  - Weinheim
PB  - Wiley-VCH
M1  - PreJuSER-38377
SP  - 431 - 436
PY  - 2004
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Bacteriorhodopsins: chemistry
KW  - Bacteriorhodopsins: metabolism
KW  - Electron Transport Complex IV: chemistry
KW  - Electron Transport Complex IV: metabolism
KW  - Membrane Proteins: chemistry
KW  - Membrane Proteins: metabolism
KW  - Rhodopsin: chemistry
KW  - Rhodopsin: metabolism
KW  - Spectrophotometry, Infrared: methods
KW  - Membrane Proteins (NLM Chemicals)
KW  - Bacteriorhodopsins (NLM Chemicals)
KW  - Rhodopsin (NLM Chemicals)
KW  - Electron Transport Complex IV (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:15185365
UR  - <Go to ISI:>//WOS:000220773500004
DO  - DOI:10.1002/cbic.200300687
UR  - https://juser.fz-juelich.de/record/38377
ER  -