Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling
Word processed copy. === Includes bibliographical references. === 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 e...
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Format: | Doctoral Thesis |
Language: | English |
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University of Cape Town
2014
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Online Access: | http://hdl.handle.net/11427/6289 |
Summary: | Word processed copy. === Includes bibliographical references. === 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. |
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