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000016351 0247_ $$2pmid$$apmid:20923666
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000016351 0247_ $$2DOI$$a10.1016/j.bpj.2010.08.017
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000016351 041__ $$aeng
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000016351 084__ $$2WoS$$aBiophysics
000016351 1001_ $$0P:(DE-HGF)0$$aInoue, R.$$b0
000016351 245__ $$aLarge domain fluctuations on 50ns timescale enable catalytic activity in phoshpglycerate kinase
000016351 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2010
000016351 300__ $$a2309 - 2317
000016351 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000016351 3367_ $$2BibTeX$$aARTICLE
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000016351 3367_ $$2DRIVER$$aarticle
000016351 440_0 $$0882$$aBiophysical Journal$$v99$$x0006-3495$$y7
000016351 500__ $$aT.R. acknowledges financial support by the International Helmholtz Research School on Biophysics and Soft Matter (BioSoft).
000016351 520__ $$aLarge-scale domain motions of enzymes are often essential for their biological function. Phosphoglycerate kinase has a wide open domain structure with a hinge near the active center between the two domains. Applying neutron spin echo spectroscopy and small-angle neutron scattering we have investigated the internal domain dynamics. Structural analysis reveals that the holoprotein in solution seems to be more compact compared to the crystal structure but would not allow the functionally important phosphoryl transfer between the substrates if the protein were static. Brownian large-scale domain fluctuation dynamics on a timescale of 50 ns was revealed by neutron spin echo spectroscopy. The dynamics observed was compared to the displacement patterns of low-frequency normal modes. The displacements along the normal-mode coordinates describe our experimental results reasonably well. In particular, the domain movements facilitate a close encounter of the key residues in the active center to build the active configuration. The observed dynamics shows that the protein has the flexibility to allow fluctuations and displacements that seem to enable the function of the protein. Moreover, the presence of the substrates increases the rigidity, which is deduced from a faster dynamics with smaller amplitude.
000016351 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
000016351 536__ $$0G:(DE-Juel1)FUEK415$$aGroßgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)$$cP55$$x1
000016351 588__ $$aDataset connected to Web of Science, Pubmed
000016351 650_2 $$2MeSH$$aBiocatalysis
000016351 650_2 $$2MeSH$$aDiffusion
000016351 650_2 $$2MeSH$$aKinetics
000016351 650_2 $$2MeSH$$aModels, Molecular
000016351 650_2 $$2MeSH$$aNeutron Diffraction
000016351 650_2 $$2MeSH$$aPhosphoglycerate Kinase: chemistry
000016351 650_2 $$2MeSH$$aPhosphoglycerate Kinase: metabolism
000016351 650_2 $$2MeSH$$aProtein Structure, Secondary
000016351 650_2 $$2MeSH$$aProtein Structure, Tertiary
000016351 650_2 $$2MeSH$$aSaccharomyces cerevisiae: enzymology
000016351 650_2 $$2MeSH$$aScattering, Small Angle
000016351 650_2 $$2MeSH$$aStructure-Activity Relationship
000016351 650_2 $$2MeSH$$aTime Factors
000016351 650_7 $$0EC 2.7.2.3$$2NLM Chemicals$$aPhosphoglycerate Kinase
000016351 650_7 $$2WoSType$$aJ
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000016351 7001_ $$0P:(DE-Juel1)130542$$aBiehl, R.$$b1$$uFZJ
000016351 7001_ $$0P:(DE-HGF)0$$aRosenkranz, T.$$b2
000016351 7001_ $$0P:(DE-HGF)0$$aFitter, J.$$b3
000016351 7001_ $$0P:(DE-Juel1)VDB2684$$aMonkenbusch, M.$$b4$$uFZJ
000016351 7001_ $$0P:(DE-Juel1)VDB4342$$aRadulescu, A.$$b5$$uFZJ
000016351 7001_ $$0P:(DE-HGF)0$$aFarago, B.$$b6
000016351 7001_ $$0P:(DE-Juel1)130917$$aRichter, D.$$b7$$uFZJ
000016351 773__ $$0PERI:(DE-600)1477214-0$$a10.1016/j.bpj.2010.08.017$$gVol. 99, p. 2309 - 2317$$n7$$p2309 - 2317$$q99<2309 - 2317$$tBiophysical journal$$v99$$x0006-3495$$y2010
000016351 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3042550
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000016351 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000016351 9141_ $$aNachtrag$$y2010
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