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Vibrational analysis of peptides, polypeptides, and proteins. VI. Assignment of Β-turn modes in insulin and other proteins

dc.contributor.authorBandekar, Jagdeeshen_US
dc.contributor.authorKrimm, Samuelen_US
dc.date.accessioned2006-04-28T16:27:15Z
dc.date.available2006-04-28T16:27:15Z
dc.date.issued1980-01en_US
dc.identifier.citationBandekar, Jagdeesh; Krimm, S. (1980)."Vibrational analysis of peptides, polypeptides, and proteins. VI. Assignment of Β-turn modes in insulin and other proteins." Biopolymers 19(1): 31-36. <http://hdl.handle.net/2027.42/37842>en_US
dc.identifier.issn0006-3525en_US
dc.identifier.issn1097-0282en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/37842
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6989414&dopt=citationen_US
dc.description.abstractThe normal modes have been calculated for structures having the dihedral angles of the four Β-turns of insulin. Frequencies are predicted in the amide I region near 1652 and 1680 cm −1 . The former overlaps the Α-helix band at 1658 cm −1 in the Raman spectrum, while the latter accounts for the hitherto unassignable band at 1681 cm −1 . Calculated amide III frequencies extend above 1300 cm −1 , providing a compelling assignment of the 1303-cm −1 band in insulin and similar bands in other globular proteins.en_US
dc.format.extent353391 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherWiley Subscription Services, Inc., A Wiley Companyen_US
dc.subject.otherChemistryen_US
dc.subject.otherPolymer and Materials Scienceen_US
dc.titleVibrational analysis of peptides, polypeptides, and proteins. VI. Assignment of Β-turn modes in insulin and other proteinsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophysics Research Division and Department of Physics, The University of Michigan, Ann Arbor, Michigan 48109en_US
dc.contributor.affiliationumBiophysics Research Division and Department of Physics, The University of Michigan, Ann Arbor, Michigan 48109en_US
dc.identifier.pmid6989414en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/37842/1/360190103_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/bip.1980.360190103en_US
dc.identifier.sourceBiopolymersen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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