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Please use this identifier to cite or link to this item: http://hdl.handle.net/2289/3161
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dc.contributor.authorKhetrapal, C.L.-
dc.contributor.authorKunwar, A.C.-
dc.date.accessioned2007-06-28T07:18:45Z-
dc.date.available2007-06-28T07:18:45Z-
dc.date.issued1981-
dc.identifier.citationJournal of Biochemical and Biophysical Methods, 1981, Vol.4, p185-190en
dc.identifier.issn0165-022X-
dc.identifier.urihttp://hdl.handle.net/2289/3161-
dc.descriptionRestricted Access.en
dc.description.abstractThe technique of 13C-NMR spectroscopy of oriented systems to problems of biological importance has been suggested and used to investigate non-planar distortions in substituted amides—models for peptides. The studies in conjunction with the proton magnetic resonance data on 15N-[13C]methyl[13C]formamide oriented in a nematic solvent provide all the direct dipolar couplings between the interacting nuclei in the system. When the 13C- and the 1H-NMR experiments are performed under non-identical conditions, 22 different direct dipolar couplings are obtained. It is demostrated that they can be used to determine unambiguously non-planar distortions around the nitrogen atom together with other geometrical data and the molecular order.en
dc.format.extent278719 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.relation.urihttp://dx.doi.org/doi:10.1016/0165-022X(81)90056-7en
dc.rights1981 Elsevier B.Ven
dc.subjectnematic phase;en
dc.subjectdirect-dipolar couplings;en
dc.subjectindirect spin-spin couplings;en
dc.subjectchemical shift;en
dc.subjectpeptide unit;en
dc.subjectdihedral anglesen
dc.titleA 13C-NMR study of non-planar distortions in amidesen
dc.typeArticleen
Appears in Collections:Research Papers (SCM)

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