Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.641852
Title: The synthesis and conformational analysis of biological molecules
Author: Boyd, Kenneth G.
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 1992
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Abstract:
This thesis discusses the synthesis and structural analysis of molecules pertinent to current problems in the areas of biosynthesis, structure activity relationships and cell biology. Chapter one investigates the structure of an N-terminal blocked derivative of methionine 5 enkephalin, in DMSO solution, using single and two dimensional nmr techniques. Analysis of the data using standard methods indicates the formation of a type I' beta turn centered around the two glycine residues. Chapter two deals with the development and optimisation of a synthesis of D,L tyrosine which is suitable for the incorporation of isotopic labels to give enriched species such as [2-13C, 15N]tyrosine which is a potentially useful biosynthesis probe. Possible uses of the probe are discussed and three routes are described. The most successful route is based on a modification of the Strecker reaction. Chapter three describes the synthesis, purification and conformational analysis of a fifteen residue peptide corresponding to the signal sequence of the hemagglutinin protein of the influenza virus A/WSN/33, the portion of the polypeptide responsible for its targeting to the cell surface. Circular dichroism studies of this N-terminal peptide in various solvents indicate that the peptide forms a predominantly β-sheet structure in aqueous solution and in alcoholic solutions of low hydrophobicity, while preferentially adopting a helical structure in more lipophilic solvent systems. The relevance of this to targeting to the cell surface is discussed.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.641852  DOI: Not available
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