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dc.contributor.authorPearce, C.M.
dc.contributor.authorWilliams, D.H.
dc.contributor.authorGerhard, Ute
dc.date.accessioned2013-11-06T09:31:04Z
dc.date.available2013-11-06T09:31:04Z
dc.date.issued1995-01-01
dc.identifier.citationPearce , C M , Williams , D H & Gerhard , U 1995 , ' Ligands which bind weakly to vancomycin : Studies by 13C NMR spectroscopy ' , Journal of the Chemical Society, Perkin Transactions 2 , no. 1 , pp. 159-162 .
dc.identifier.issn1472-779X
dc.identifier.otherPURE: 848599
dc.identifier.otherPURE UUID: 644c73ea-eaaf-4095-9bdc-1b19d0317ec0
dc.identifier.otherScopus: 37049082456
dc.identifier.urihttp://hdl.handle.net/2299/11997
dc.descriptionCopyright 2007 Elsevier B.V., All rights reserved.
dc.description.abstractC NMR chemical shifts of vancomycin have been used to obtain the association constants for a number of ligands which bind weakly to the antibiotic. The change in these C chemical shifts upon stepwise addition of ligands provides evidence that the ligands bind in a manner analogous to natural cell-wall precursor analogues. The binding constants obtained are in good agreement with those determined earlier by other methods. Where the ligands are amino acids (glycine or alanine), a potential alkylammonium to amide carbonyl interaction does not promote binding.en
dc.format.extent4
dc.language.isoeng
dc.relation.ispartofJournal of the Chemical Society, Perkin Transactions 2
dc.titleLigands which bind weakly to vancomycin : Studies by 13C NMR spectroscopyen
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.description.statusPeer reviewed
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=37049082456&partnerID=8YFLogxK
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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