Direct observation of correlated interdomain motion in alcohol dehydrogenase

Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spin-echo spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the clef...

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Bibliographic Details
Published inPhysical review letters Vol. 101; no. 13; p. 138102
Main Authors Biehl, Ralf, Hoffmann, Bernd, Monkenbusch, Michael, Falus, Peter, Préost, Sylvain, Merkel, Rudolf, Richter, Dieter
Format Journal Article
LanguageEnglish
Published United States 26.09.2008
Subjects
Alcohol Dehydrogenase - chemistry
Alcohol Dehydrogenase - metabolism
Models, Chemical
Models, Molecular
NAD - chemistry
NAD - metabolism
Protein Structure, Tertiary
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Temperature
Thermodynamics
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Summary:Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spin-echo spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor.
ISSN:0031-9007
DOI:10.1103/physrevlett.101.138102