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001     201686
005     20240619092010.0
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024 7 _ |a 1347-4073
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082 _ _ |a 530
100 1 _ |a Stadler, Andreas
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245 _ _ |a Neutron Spin-Echo and TOF Reveals Protein Dynamics in Solution
260 _ _ |a Tokyo
|c 2013
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336 7 _ |a Journal Article
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520 _ _ |a The ps to ns dynamics of the protein alcohol dehydrogenase (ADH) has been measured in dilute solution by time-of-flight (TOF) neutron spectroscopy. The investigation extends previous experiments on ADH solutions with neutron-spin-echo spectroscopy. The interpretation of TOF experiments used the diffusion data from NSE as input to decribe the observed slow component of the quasielastic spectra, in addition a fast component to be associated to mobile groups in the protein could be observed. The description within a simple model for translational and rotational diffusion and a fraction of protons with confined local mobility is given together with a novel method to accurately and efficiently account for the instrumental resolution.
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700 1 _ |a Monkenbusch, Michael
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700 1 _ |a Biehl, Ralf
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700 1 _ |a Richter, Dieter
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700 1 _ |a Ollivier, Jacques
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773 _ _ |a 10.7566/JPSJS.82SA.SA016
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