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A study of a C Α, Β -didehydroalanine homo-oligopeptide series in the solid-state by 13 C cross-polarization magic angle spinning NMR
dc.contributor.authorHenzler Wildman, Katherine A.en_US
dc.contributor.authorRamamoorthy, Ayyalusamyen_US
dc.contributor.authorWakamiya, Tateakien_US
dc.contributor.authorYoshikawa, Taichien_US
dc.contributor.authorCrisma, Marcoen_US
dc.contributor.authorToniolo, Claudioen_US
dc.contributor.authorFormaggio, Fernandoen_US
dc.date.accessioned2006-04-19T14:15:57Z
dc.date.available2006-04-19T14:15:57Z
dc.date.issued2004-06en_US
dc.identifier.citationHenzler Wildman, Katherine A.; Ramamoorthy, Ayyalusamy; Wakamiya, Tateaki; Yoshikawa, Taichi; Crisma, Marco; Toniolo, Claudio; Formaggio, Fernando (2004)."A study of a C Α, Β -didehydroalanine homo-oligopeptide series in the solid-state by 13 C cross-polarization magic angle spinning NMR." Journal of Peptide Science 10(6): 336-341. <http://hdl.handle.net/2027.42/35198>en_US
dc.identifier.issn1075-2617en_US
dc.identifier.issn1099-1387en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/35198
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=15214438&dopt=citationen_US
dc.description.abstractThe fully extended peptide conformation (2.0 5 -helix) has been investigated for the first time in the solid-state by 13 C cross-polarization magic angle spinning NMR. The compounds examined are members of a terminally protected, homo-oligopeptide series (from monomer through hexamer) based on C Α, Β -didehydroalanine. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.en_US
dc.format.extent100441 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherJohn Wiley & Sons, Ltd.en_US
dc.subject.otherChemistryen_US
dc.subject.otherBiochemistry and Biotechnologyen_US
dc.titleA study of a C Α, Β -didehydroalanine homo-oligopeptide series in the solid-state by 13 C cross-polarization magic angle spinning NMRen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USAen_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA ; Biophysics Research Division, University of Michigan, Ann Arbor, MI 48109-1055, USA ; Macromolecular Science and Engineering, University of Michigan, Ann Arbor, MI 48109-1055, USA ; Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USAen_US
dc.contributor.affiliationotherDepartment of Chemistry, Faculty of Science and Technology, Kinki University, Osaka 577, 8502 Japanen_US
dc.contributor.affiliationotherDepartment of Chemistry, Faculty of Science and Technology, Kinki University, Osaka 577, 8502 Japanen_US
dc.contributor.affiliationotherInstitute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italyen_US
dc.contributor.affiliationotherInstitute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italyen_US
dc.contributor.affiliationotherInstitute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italyen_US
dc.identifier.pmid15214438en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/35198/1/551_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/psc.551en_US
dc.identifier.sourceJournal of Peptide Scienceen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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