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Interproton distance restraints were calculated from measured NOe crosspeak intensities for each peptide."]},{"key":"dc:title","label":"Title","values":["Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling"]}]}],"canonical_facts":{"dc:contributor.advisor":["Jackson, Graham Ellis"],"dc:creator":["Stone, Shane Ramsay"],"dc:date.accessioned":["2014-08-13T14:25:47Z"],"dc:date.available":["2014-08-13T14:25:47Z"],"dc:date.issued":["2006"],"dc:description":["Word processed copy.","Includes bibliographical references."],"dc:description.abstract":["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. 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