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Normal mode spectrum of the parallel-chain Β-sheet This is paper number 39 in a series on “Vibrational Analysis of Peptides, Polypeptides, and Proteins,” of which paper number 38 is Ref. 19.

dc.contributor.authorBandekar, Jagdeeshen_US
dc.contributor.authorKrimm, Samuelen_US
dc.date.accessioned2006-04-28T16:27:54Z
dc.date.available2006-04-28T16:27:54Z
dc.date.issued1988-06en_US
dc.identifier.citationBandekar, Jagdeesh; Krimm, S. (1988)."Normal mode spectrum of the parallel-chain Β-sheet This is paper number 39 in a series on “Vibrational Analysis of Peptides, Polypeptides, and Proteins,” of which paper number 38 is Ref. 19. ." Biopolymers 27(6): 909-921. <http://hdl.handle.net/2027.42/37855>en_US
dc.identifier.issn0006-3525en_US
dc.identifier.issn1097-0282en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/37855
dc.description.abstractNormal mode calculations have been carried out for parallel-chain Β-sheet structures. These include the parallel-chain pleated sheet of poly( L -alanine) and the parallel-chain rippled sheet of polyglycine. Dipole derivative coupling has been included for amide I and II modes, and the effects of parallel-sheet and antiparallel-sheet arrangements of varying separation have been examined for the poly( L -alanine) case. Some amide and nonamide modes are distinctly different from their antiparallel-chain counterparts, thus providing a basis for distinguishing between such structures from their ir and Raman spectra. As in our previous studies, these results emphasize the need for both kinds of spectral data in order to draw definitive conclusions about conformation.en_US
dc.format.extent700139 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.titleNormal mode spectrum of the parallel-chain Β-sheet This is paper number 39 in a series on “Vibrational Analysis of Peptides, Polypeptides, and Proteins,” of which paper number 38 is Ref. 19.en_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, University of Michigan, Ann Arbor, Michigan 48109en_US
dc.contributor.affiliationumBiophysics Research Division and Department of Physics, University of Michigan, Ann Arbor, Michigan 48109en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/37855/1/360270603_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/bip.360270603en_US
dc.identifier.sourceBiopolymersen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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