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Title: The synthesis and conformational analysis of mitochondrial targeting peptides
Author: Pitkeathly, Maureen C.
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 1991
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The thesis discusses protein targeting within cells, and in particular targeting to the mitochondrion. The synthesis and conformational analysis by CD and NMR of a mitochondrial targeting presequence peptide, and a non-functional deletion peptide are described. The intramitochondrial sorting of proteins is also discussed and investigated. Ch. 1 reviews the currently available knowledge of the mechanisms and factors involved in protein targeting. Ch. 2 describes the synthesis and purification of the 25 residue peptide corresponding to the mitochondrial targeting presequence of subunit IV of yeast cytochrome oxidase. Ch. 3 describes the conformational analysis by CD and NMR studies of the synthetic peptide and discusses the structural information that can be drawn from the data. Both sets of data indicate that the peptide appears to adopt a partially helical structure. Ch. 4 describes the synthesis and purification of a 23 residue peptide corresponding to a non-functional deletion mutation of the cytochrome oxidase subunit IV targeting peptide. The CD and NNR studies carried out on this peptide, the preliminary results of which indicate an absence of any regular structural motifs, are discussed. Ch. 5 reviews the current understanding of the mechanisms of intramitochondrial sorting and their evolutionary relationship to protein secretion. E.Coli cells expressing cytochrome b2 with various portions of the presequence removed were subfractioned to determine whether any form of the presequence showed a strong tendency to target the protein to the cell membranes. Conclusive results were not obtained due to the formation of inclusion bodies within the cells.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available