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001     16351
005     20240619092122.0
024 7 _ |2 pmid
|a pmid:20923666
024 7 _ |2 pmc
|a pmc:PMC3042550
024 7 _ |2 DOI
|a 10.1016/j.bpj.2010.08.017
024 7 _ |2 WOS
|a WOS:000282850600037
024 7 _ |2 MLZ
|a InoueBRFMRFR2010
037 _ _ |a PreJuSER-16351
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biophysics
100 1 _ |0 P:(DE-HGF)0
|a Inoue, R.
|b 0
245 _ _ |a Large domain fluctuations on 50ns timescale enable catalytic activity in phoshpglycerate kinase
260 _ _ |a New York, NY
|b Rockefeller Univ. Press
|c 2010
300 _ _ |a 2309 - 2317
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |0 882
|a Biophysical Journal
|v 99
|x 0006-3495
|y 7
500 _ _ |a T.R. acknowledges financial support by the International Helmholtz Research School on Biophysics and Soft Matter (BioSoft).
520 _ _ |a Large-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.
536 _ _ |0 G:(DE-Juel1)FUEK505
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|a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
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536 _ _ |0 G:(DE-Juel1)FUEK415
|a Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)
|c P55
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Biocatalysis
650 _ 2 |2 MeSH
|a Diffusion
650 _ 2 |2 MeSH
|a Kinetics
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Neutron Diffraction
650 _ 2 |2 MeSH
|a Phosphoglycerate Kinase: chemistry
650 _ 2 |2 MeSH
|a Phosphoglycerate Kinase: metabolism
650 _ 2 |2 MeSH
|a Protein Structure, Secondary
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Saccharomyces cerevisiae: enzymology
650 _ 2 |2 MeSH
|a Scattering, Small Angle
650 _ 2 |2 MeSH
|a Structure-Activity Relationship
650 _ 2 |2 MeSH
|a Time Factors
650 _ 7 |0 EC 2.7.2.3
|2 NLM Chemicals
|a Phosphoglycerate Kinase
650 _ 7 |2 WoSType
|a J
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|a Forschungs-Neutronenquelle Heinz Maier-Leibnitz
|e KWS-1: Small angle scattering diffractometer
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700 1 _ |0 P:(DE-Juel1)130542
|a Biehl, R.
|b 1
|u FZJ
700 1 _ |0 P:(DE-HGF)0
|a Rosenkranz, T.
|b 2
700 1 _ |0 P:(DE-HGF)0
|a Fitter, J.
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700 1 _ |0 P:(DE-Juel1)VDB2684
|a Monkenbusch, M.
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700 1 _ |0 P:(DE-Juel1)VDB4342
|a Radulescu, A.
|b 5
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700 1 _ |0 P:(DE-HGF)0
|a Farago, B.
|b 6
700 1 _ |0 P:(DE-Juel1)130917
|a Richter, D.
|b 7
|u FZJ
773 _ _ |0 PERI:(DE-600)1477214-0
|a 10.1016/j.bpj.2010.08.017
|g Vol. 99, p. 2309 - 2317
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|p 2309 - 2317
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|t Biophysical journal
|v 99
|x 0006-3495
|y 2010
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3042550
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|v Neutrons for Research on Condensed Matter
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914 1 _ |a Nachtrag
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915 _ _ |0 StatID:(DE-HGF)0010
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