The influence of cofactor binding on thermal fluctuations of alcohol dehydrogenase studied by using quasielastic neutron scattering
Large scale amplitude domain motions have been observed in the protein alcohol dehydrogenase (ADH) using neutron spin-echo spectroscopy. Binding of the small cofactor nicotinamide adenine dinucleotide (NADH) resulted in an apparent reduction of the diffusion coefficients of the collective domain motions. One hypothesis, which we would like to test, is whether fast localized protein fluctuations are related to the collective domain motions. In this proposal we propose to investigate using the IN5 spectrometer whether localised thermal fluctuations in the protein ADH are influenced by binding of the cofactor NADH. The IN5 instrument would be set to two resolutions covering the 100ps time scale, which is associated with slow localized dynamics in proteins, and the ps time scale, which is associated with fast amino acid side chain motions. We expect that this will shed light to connections between localized thermal motions and collective domain motions.
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Andreas M. Stadler; BIEHL Ralf; MONKENBUSCH Michael; OLLIVIER Jacques and RICHTER Dieter. (2013). The influence of cofactor binding on thermal fluctuations of alcohol dehydrogenase studied by using quasielastic neutron scattering. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-684
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