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000000541 1001_ $$0P:(DE-Juel1)130542$$aBiehl, R.$$b0$$uFZJ
000000541 245__ $$aDirect Observation of Correlated Interdomain Motion in Alcohol Dehydrogenase
000000541 260__ $$aCollege Park, Md.$$bAPS$$c2008
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000000541 520__ $$aInterdomain motions in proteins are essential to enable or promote biochemical function. Neutron spinecho spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor.
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000000541 8567_ $$uhttp://dx.doi.org/10.1103/PhysRevLett.101.138102
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