A conformational analysis of signal peptides

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dc.contributor.authorChantson, Tracy, Elizabeth
dc.date.accessioned2017-04-19T10:42:47Z
dc.date.available2017-04-19T10:42:47Z
dc.date.issued1998
dc.descriptionA thesis submitted to the Faculty of Science University of the Witwatersrand in fulfillment of the requirements for the degree of Doctor of Philosophy. Johannesburg, 1998.en_ZA
dc.description.abstractConformational analysis of portions of functionally-active and functionally-inactive signal peptides (incorporating the wild-type and mutants thereof) has been performed using a variety of computational prediction techniques based on both statistics and molecular mechanics. Molecular mechanics conformational studies are generally plagued by the problem of combinatorial explosion; this problem was addressed with a systematic searching procedure as well as a recently developed genetic algorithm, both utilising tile ECEPP/3 force field. The genetic algorithm, in combination with a gradient minimiser, proved to be successful in finding low-energy conformations for each peptide sequence studied. Analysis was performed in both simulated hydrophobic and hydrophilic environments, under distance-constraints. The molecular mechanics results and statistical predictions generated from the study were compared With existing experimental observations. The reliability of statistical predictions proved to be dependent on prediction method; the more consistent predictions were produced by methods based on membrane proteins, as opposed to those based on globular proteins. The physical property of hydrophobicity of signal peptide sequences, explored in these statistical predictions, was determined to be an important factor in relating sequence to functional activity. Molecular mechanics calculations produced either interrupted or non interrupted a-helical secondary structures both for functionally-efficient and for functionally-inefficient signal peptides, indicating that cc-helixformation alone cannot be correlated with protein export competence. It was concluded from our overall results that both a-helicity and hydrophobicity are required for the efficient functioning of signal peptides.en_ZA
dc.description.librarianAC2017en_ZA
dc.format.extentOnline resource (156 leaves)
dc.identifier.citationChantson, Tracy, Elizabeth (1998) A conformational analysis of signal peptides, University of the Witwatersrand, Johannesburg, <http://hdl.handle.net/10539/22402>
dc.identifier.urihttp://hdl.handle.net/10539/22401
dc.language.isoenen_ZA
dc.subject.lcshPeptides
dc.subject.lcshMolecules--Models--Data processing
dc.subject.lcshMolecular structure
dc.titleA conformational analysis of signal peptidesen_ZA
dc.typeThesisen_ZA
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