Structural studies on the mitochondrial and bacterial F1Fo-ATP synthase

Colin Thompson

    Research output: ThesisDoctoral Thesis

    5 Downloads (Pure)

    Abstract

    [Truncated] ATP synthase is the enzyme responsible for the production of the majority of cellular ATP. This fundamental process is essential for all life and, aptly, is a focal point of intense research. The studies presented in this thesis investigate both the structure and regulation of ATP synthase. A summary of the experimental findings is as follows; Chapter 3 aimed to elucidate the structure of subunit h from yeast mitochondrial ATP synthase. Chapter 4 aimed to investigate the interface between the F1 and F0 sectors of E. coli ATP synthase. Chapter 5 employed the use of mutagenesis to probe the interface between the y and E subunits in order to identify key amino acid residues involved in orientating and maintaining the extended form of the E subunit C-terminal helices. Chapter 6 investigates the effect of pH on the structure of the y'E complex.
    Original languageEnglish
    QualificationDoctor of Philosophy
    Awarding Institution
    • The University of Western Australia
    DOIs
    Publication statusUnpublished - 2006

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