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Study of protein dynamics in solution by measurement of 13 C α - 13 CO NOE and 13 CO longitudinal relaxation
dc.contributor.authorZeng, Leien_US
dc.contributor.authorFischer, Mark W. F.en_US
dc.contributor.authorZuiderweg, Erik R. P.en_US
dc.date.accessioned2006-09-08T21:00:55Z
dc.date.available2006-09-08T21:00:55Z
dc.date.issued1996-03en_US
dc.identifier.citationZeng, Lei; Fischer, Mark W. F.; Zuiderweg, Erik R. P.; (1996). "Study of protein dynamics in solution by measurement of 13 C α - 13 CO NOE and 13 CO longitudinal relaxation." Journal of Biomolecular NMR 7(2): 157-162. <http://hdl.handle.net/2027.42/43052>en_US
dc.identifier.issn0925-2738en_US
dc.identifier.issn1573-5001en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/43052
dc.description.abstract13 C α - 13 CO homonuclear NOE and 13 CO T 1 relaxation were measured for a 20 kDa protein using tripleresonance pulse sequences. The experiments were sufficiently sensitive to obtain statistically significant differences in relaxation parameters over the molecule. The 13 C α - 13 CO cross-relaxation rate, obtained from these data, is directly proportional to an order parameter describing local motion and it is largely independent of the local correlation time. It is therefore a relatively straightforward observable for the identification of local dynamics.en_US
dc.format.extent475471 bytes
dc.format.extent3115 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherKluwer Academic Publishers; ESCOM Science Publishers B.V. ; Springer Science+Business Mediaen_US
dc.subject.otherChemistryen_US
dc.subject.otherPolymer Sciencesen_US
dc.subject.otherAnimal Anatomy / Morphology / Histologyen_US
dc.subject.otherC α CO NOEen_US
dc.subject.otherTriple-resonance NMRen_US
dc.subject.otherLongitudinal Relaxationen_US
dc.subject.otherCarbonyl NMRen_US
dc.subject.otherOrder Parametersen_US
dc.subject.otherT4-lysozymeen_US
dc.titleStudy of protein dynamics in solution by measurement of 13 C α - 13 CO NOE and 13 CO longitudinal relaxationen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophysics Research Division, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumBiophysics Research Division, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USA; Department of Physics, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumBiophysics Research Division, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USA; Department of Biological Chemistry, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumcampusAnn Arboren_US
dc.identifier.pmid22911008en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/43052/1/10858_2004_Article_BF00203826.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1007/BF00203826en_US
dc.identifier.sourceJournal of Biomolecular NMRen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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