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000011981 0247_ $$2DOI$$a10.1002/cphc.200900514
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000011981 041__ $$aeng
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000011981 084__ $$2WoS$$aChemistry, Physical
000011981 084__ $$2WoS$$aPhysics, Atomic, Molecular & Chemical
000011981 1001_ $$0P:(DE-Juel1)VDB2684$$aMonkenbusch, M.$$b0$$uFZJ
000011981 245__ $$aObservation of protein domain motions by neutron spectroscopy
000011981 260__ $$aWeinheim$$bWiley-VCH Verl.$$c2010
000011981 300__ $$a1187 - 1194
000011981 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000011981 440_0 $$010582$$aChemPhysChem$$v11$$x1439-4235$$y6
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000011981 520__ $$aHigh-resolution inelastic neutron scattering, which is available with neutron spin-echo spectroscopy (NSE) is introduced as a tool for the analysis of biomolecule flexibility. Coherent scattering in a range where it is sensitive to length scales of nanometers and covering a time range from picoseconds to several 100 ns makes the motion of larger subdomains within proteins visible. We show that and how the internal domain motion within a protein in solution can be measured. Comparison with displacement patterns from normal mode analysis provides further insight into the nature of the geometry of the motions that lead to the observed dynamic signature. The NSE experiment on alcohol dehydrogenase (ADH) is used as example to illustrate the general principles of the method.
000011981 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
000011981 536__ $$0G:(DE-Juel1)FUEK415$$aGroßgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)$$cP55$$x1
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000011981 65320 $$2Author$$aconformation analysis
000011981 65320 $$2Author$$aneutron scattering
000011981 65320 $$2Author$$aneutron spectroscopy
000011981 65320 $$2Author$$aprotein domain motions
000011981 65320 $$2Author$$aprotein structures
000011981 650_2 $$2MeSH$$aAlcohol Dehydrogenase: chemistry
000011981 650_2 $$2MeSH$$aMolecular Dynamics Simulation
000011981 650_2 $$2MeSH$$aNAD: chemistry
000011981 650_2 $$2MeSH$$aNeutron Diffraction
000011981 650_2 $$2MeSH$$aProtein Structure, Tertiary
000011981 650_7 $$053-84-9$$2NLM Chemicals$$aNAD
000011981 650_7 $$0EC 1.1.1.1$$2NLM Chemicals$$aAlcohol Dehydrogenase
000011981 650_7 $$2WoSType$$aJ
000011981 7001_ $$0P:(DE-Juel1)130917$$aRichter, D.$$b1$$uFZJ
000011981 7001_ $$0P:(DE-Juel1)130542$$aBiehl, R.$$b2$$uFZJ
000011981 773__ $$0PERI:(DE-600)2025223-7$$a10.1002/cphc.200900514$$gVol. 11, p. 1187 - 1194$$p1187 - 1194$$q11<1187 - 1194$$tChemPhysChem$$v11$$x1439-4235$$y2010
000011981 8567_ $$uhttp://dx.doi.org/10.1002/cphc.200900514
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000011981 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000011981 9141_ $$y2010
000011981 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x0
000011981 9131_ $$0G:(DE-Juel1)FUEK415$$bStruktur der Materie$$kP55$$lGroßgeräteforschung mit Photonen, Neutronen und Ionen$$vGroßgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)$$x1
000011981 9132_ $$0G:(DE-HGF)POF3-623$$1G:(DE-HGF)POF3-620$$2G:(DE-HGF)POF3-600$$aDE-HGF$$bForschungsbereich Materie$$lIn-house research on the structure, dynamics and function of matter$$vNeutrons for Research on Condensed Matter$$x0
000011981 9201_ $$0I:(DE-Juel1)VDB784$$d31.12.2010$$gIFF$$kIFF-4$$lStreumethoden$$x1
000011981 9201_ $$0I:(DE-Juel1)VDB785$$d31.12.2010$$gIFF$$kIFF-5$$lNeutronenstreuung$$x0
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