| Literature DB >> 15185365 |
Rebecca M Nyquist1, Kenichi Ataka, Joachim Heberle.
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.Mesh:
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Year: 2004 PMID: 15185365 DOI: 10.1002/cbic.200300687
Source DB: PubMed Journal: Chembiochem ISSN: 1439-4227 Impact factor: 3.164