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Letter to the Editor: 1H, 15N and 13C assignments of the N-terminal domain of Yersinia outer protein H in its apo form and in complex with a phosphotyrosine peptide

dc.contributor.authorKhandelwal, Purnimaen_US
dc.contributor.authorKeliikuli, Kaien_US
dc.contributor.authorSmith, Craig L.en_US
dc.contributor.authorSaper, Mark A.en_US
dc.contributor.authorZuiderweg, Erik R. P.en_US
dc.date.accessioned2006-09-08T21:00:28Z
dc.date.available2006-09-08T21:00:28Z
dc.date.issued2001-09en_US
dc.identifier.citationKhandelwal, Purnima; Keliikuli, Kai; Smith, Craig L.; Saper, Mark A.; Zuiderweg, Erik R.P.; (2001). "Letter to the Editor: 1H, 15N and 13C assignments of the N-terminal domain of Yersinia outer protein H in its apo form and in complex with a phosphotyrosine peptide." Journal of Biomolecular NMR 21(1): 69-70. <http://hdl.handle.net/2027.42/43045>en_US
dc.identifier.issn0925-2738en_US
dc.identifier.issn1573-5001en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/43045
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11693571&dopt=citationen_US
dc.format.extent53810 bytes
dc.format.extent3115 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherKluwer Academic Publishers; Springer Science+Business Mediaen_US
dc.subject.otherChemistryen_US
dc.subject.otherPolymer Sciencesen_US
dc.subject.otherAnimal Anatomy / Morphology / Histologyen_US
dc.subject.otherHeteronuclear NMRen_US
dc.subject.otherPeptide Complexen_US
dc.subject.otherSequential Assignmenten_US
dc.subject.otherYopHen_US
dc.titleLetter to the Editor: 1H, 15N and 13C assignments of the N-terminal domain of Yersinia outer protein H in its apo form and in complex with a phosphotyrosine peptideen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophysics Research Division and Departments of, University of Michigan, 930 N. University Ave., Ann Arbor, MI, 48109-1055, U.S.Aen_US
dc.contributor.affiliationumBiophysics Research Division and Departments of, University of Michigan, 930 N. University Ave., Ann Arbor, MI, 48109-1055, U.S.Aen_US
dc.contributor.affiliationumBiophysics Research Division and Departments, USA; Biological Chemistry, University of Michigan, 930 N. University Ave., Ann Arbor, MI, 48109-1055, U.S.Aen_US
dc.contributor.affiliationumBiophysics Research Division and Departments, USA; Biological Chemistry, University of Michigan, 930 N. University Ave., Ann Arbor, MI, 48109-1055, U.S.Aen_US
dc.contributor.affiliationumBiophysics Research Division and Departments of, USA; Biological Chemistry, USA; Chemistry, University of Michigan, 930 N. University Ave., Ann Arbor, MI, 48109-1055, U.S.Aen_US
dc.contributor.affiliationumcampusAnn Arboren_US
dc.identifier.pmid11693571en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/43045/1/10858_2004_Article_359237.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1023/A:1011971202626en_US
dc.identifier.sourceJournal of Biomolecular NMRen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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