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dc.creatorSen, A. C.en_US
dc.creatorKeiderling, T. A.en_US
dc.date.accessioned2006-06-15T14:47:42Z
dc.date.available2006-06-15T14:47:42Z
dc.date.issued1983en_US
dc.identifier1983-RC-06en_US
dc.identifier.urihttp://hdl.handle.net/1811/11879
dc.descriptionAuthor Institution: Department of Chemistry, University of Illinoisen_US
dc.description.abstractVCD spectra of some of the $\alpha$-helical polypeptides, both normal and deuterated, have been recorded in the Amide I and Amide II region. The most striking effect of complete deuteration is the characteristic shift in absorption and VCD spectra as well as change in the VCD shape in some cases. The sign of VCD depends only on the sense of helicity of the $\alpha$-helix, being not affected by deuteration. Attempts will be made to analyse the anomalies in the observed spectra.en_US
dc.format.extent49257 bytes
dc.format.mimetypeimage/jpeg
dc.language.isoEnglishen_US
dc.publisherOhio State Universityen_US
dc.titleTHE EFFECT OF DEUTERATION ON THE AMIDE I \& II BANDS OF $\alpha$-HELICAL POLYPEPTIDES AS EVIDENCED BY VCD STUDIESen_US
dc.typearticleen_US


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