Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling

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dc.contributor.advisorJackson, Graham Ellisen_ZA
dc.contributor.authorStone, Shane Ramsayen_ZA
dc.date.accessioned2014-08-13T14:25:47Z
dc.date.available2014-08-13T14:25:47Z
dc.date.issued2006en_ZA
dc.descriptionWord processed copy.en_ZA
dc.descriptionIncludes bibliographical references.en_ZA
dc.description.abstractThe solution studies aimed to determine the conformations of a series of DMSO solubilised gastrin peptides, G-4, [ß-Ala ¹] G-5 and G-17, so as to establish how the configurations of the biologically relevant sequence were related to each other, and to resolve whether they adopted preferred and conserved conformations in solution. Interproton distance restraints were calculated from measured NOe crosspeak intensities for each peptide.en_ZA
dc.identifier.apacitationStone, S. R. (2006). <i>Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling</i>. (Thesis). University of Cape Town ,Faculty of Science ,Department of Chemistry. Retrieved from http://hdl.handle.net/11427/6289en_ZA
dc.identifier.chicagocitationStone, Shane Ramsay. <i>"Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling."</i> Thesis., University of Cape Town ,Faculty of Science ,Department of Chemistry, 2006. http://hdl.handle.net/11427/6289en_ZA
dc.identifier.citationStone, S. 2006. Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling. University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Stone, Shane Ramsay AB - The solution studies aimed to determine the conformations of a series of DMSO solubilised gastrin peptides, G-4, [ß-Ala ¹] G-5 and G-17, so as to establish how the configurations of the biologically relevant sequence were related to each other, and to resolve whether they adopted preferred and conserved conformations in solution. Interproton distance restraints were calculated from measured NOe crosspeak intensities for each peptide. DA - 2006 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 2006 T1 - Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling TI - Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling UR - http://hdl.handle.net/11427/6289 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/6289
dc.identifier.vancouvercitationStone SR. Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling. [Thesis]. University of Cape Town ,Faculty of Science ,Department of Chemistry, 2006 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/6289en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDepartment of Chemistryen_ZA
dc.publisher.facultyFaculty of Scienceen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherChemistryen_ZA
dc.titleStructural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modellingen_ZA
dc.typeDoctoral Thesis
dc.type.qualificationlevelDoctoral
dc.type.qualificationnamePhDen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
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