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

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.

Grantor dc:publisher.institution

Department of Chemistry

Year dc:date.issued

2006

Author dc:creator

• Stone, Shane Ramsay

Advisor dc:contributor.advisor

• Jackson, Graham Ellis

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/11427/6289

OAI identifier oai:identifier

oai:open.uct.ac.za:11427/6289