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000000275 0247_ $$2DOI$$a10.1007/s10858-008-9229-3
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000000275 084__ $$2WoS$$aBiochemistry & Molecular Biology
000000275 084__ $$2WoS$$aSpectroscopy
000000275 1001_ $$0P:(DE-HGF)0$$aGardiennet, C.$$b0
000000275 245__ $$aStructural constraints for the Crh protein from solid-state NMR experiments
000000275 260__ $$aDordrecht [u.a.]$$bSpringer Science + Business Media B.V$$c2008
000000275 300__ $$a239 - 250
000000275 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000000275 440_0 $$09165$$aJournal of Biomolecular NMR$$v40$$x0925-2738$$y4
000000275 500__ $$aRecord converted from VDB: 12.11.2012
000000275 520__ $$aWe demonstrate that short, medium and long-range constraints can be extracted from proton mediated, rare-spin detected correlation solid-state NMR experiments for the microcrystalline 10.4 x 2 kDa dimeric model protein Crh. Magnetization build-up curves from cross signals in NHHC and CHHC spectra deliver detailed information on side chain conformers and secondary structure for interactions between spin pairs. A large number of medium and long-range correlations can be observed in the spectra, and an analysis of the resolved signals reveals that the constraints cover the entire sequence, also including inter-monomer contacts between the two molecules forming the domain-swapped Crh dimer. Dynamic behavior is shown to have an impact on cross signals intensities, as indicated for mobile residues or regions by contacts predicted from the crystal structure, but absent in the spectra. Our work validates strategies involving proton distance measurements for large and complex proteins as the Crh dimer, and confirms the magnetization transfer properties previously described for small molecules in solid protein samples.
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000000275 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000000275 650_2 $$2MeSH$$aDimerization
000000275 650_2 $$2MeSH$$aModels, Molecular
000000275 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular: methods
000000275 650_2 $$2MeSH$$aPhosphoproteins: chemistry
000000275 650_2 $$2MeSH$$aProtein Conformation
000000275 650_2 $$2MeSH$$aProtons
000000275 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000000275 650_7 $$00$$2NLM Chemicals$$aCrh protein, Bacillus subtilis
000000275 650_7 $$00$$2NLM Chemicals$$aPhosphoproteins
000000275 650_7 $$00$$2NLM Chemicals$$aProtons
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000000275 65320 $$2Author$$acatabolite repression histidine-containing phosphocarrier protein (Crh)
000000275 65320 $$2Author$$adistance constraints
000000275 65320 $$2Author$$aMAS
000000275 65320 $$2Author$$a3D protein structure
000000275 65320 $$2Author$$asolid-state NMR spectroscopy
000000275 7001_ $$0P:(DE-HGF)0$$aLoquet, A.$$b1
000000275 7001_ $$0P:(DE-HGF)0$$aBockmann, A$$b2
000000275 7001_ $$0P:(DE-HGF)0$$aEtzkorn, M.$$b3
000000275 7001_ $$0P:(DE-Juel1)VDB77857$$aHeise, H.$$b4$$uFZJ
000000275 7001_ $$0P:(DE-HGF)0$$aBaldus, M.$$b5
000000275 773__ $$0PERI:(DE-600)2006645-4$$a10.1007/s10858-008-9229-3$$gVol. 40, p. 239 - 250$$p239 - 250$$q40<239 - 250$$tJournal of biomolecular NMR$$v40$$x0925-2738$$y2008
000000275 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2579321
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000000275 9141_ $$y2008
000000275 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000000275 9201_ $$0I:(DE-Juel1)VDB805$$d31.12.2008$$gINB$$kINB-2$$lMolekulare Biophysik$$x0
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