Enzyme Conformational Dynamics During Catalysis and in the 'resting State' Monitored by Hydrogen/Deuterium Exchange Mass Spectrometry.
From: Department of Chemistry, The University of Western Ontario, London, Ont., Canada N6A 5B7.
FEBS letters
- Publish Date: Oct 2006
- ISSN: 0014-5793
- Volume: 580
- Issue: 22
- Pages: 5137-42
- Medium: Print
- Language: English
- Citation (JAMA): Liu Yu-Hong, Konermann Lars, et al. Enzyme Conformational Dynamics During Catalysis and in the 'resting State' Monitored by Hydrogen/Deuterium Exchange Mass Spectrometry.. FEBS Lett. Oct 2006;580:5137-42
Abstract
This work reports the use of electrospray mass spectrometry for studying the conformational dynamics of enzymes by amide hydrogen/deuterium exchange (HDX) measurements. A rapid-mixing quench-flow approach allows comparisons to be made between the HDX kinetics of free enzymes with those under steady-state conditions. Experiments carried out on carboxypeptidase B in the absence of substrate and in the presence of saturating concentrations of hippuryl-Arg result in HDX kinetics that are indistinguishable. This finding implies that the conformational dynamics that mediate HDX are not significantly different in the resting state of the enzyme and during substrate turnover.
Mesh Headings (Keywords): Animals, Arginine, Carboxypeptidase B, Catalysis, Chickens, Deuterium, Deuterium Exchange Measurement, Muramidase, Protein Conformation, Spectrometry, Mass, Electrospray Ionization, Swine
Check for Full Text / PubMed Unique Identifier (PMID): 16963025
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.