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Enzyme Conformational Dynamics During Catalysis and in the 'Resting State' Monitored by hydrogen/deuterium Exchange Mass Spectrometry

Enzyme Conformational Dynamics During Catalysis and in the 'Resting State' Monitored by hydrogen/deuterium Exchange Mass Spectrometry

Yu-Hong Liu, Lars Konermann

FEBS Lett. 2006 Oct 2;580(22):5137-42.

PMID: 16963025

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP744467	Hippuryl-Arg		744-46-7	Price

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