The molecular mechanism of membrane proteins probed by evanescent infrared waves.
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.
Nyquist
Rebecca M
RM
Forschungszentrum Jülich, IBI-2: Structural Biology, 52425 Jülich, Germany.
Ataka
Kenichi
K
Heberle
Joachim
J
D001436:Bacteriorhodopsins / Q000737:chemistry / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D012243:Rhodopsin / Q000737:chemistry / Q000378:metabolism; D013055:Spectrophotometry, Infrared / Q000379:methods*
D008565:Membrane Proteins; D001436:Bacteriorhodopsins; D012243:Rhodopsin; D003576:Electron Transport Complex IV