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Biophysical studies of intracellular signal transduction proteins: Investigating the structure-function relationship

Bottomley, Matthew James; (1998) Biophysical studies of intracellular signal transduction proteins: Investigating the structure-function relationship. Doctoral thesis (Ph.D), UCL (University College London). Green open access

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Abstract

This thesis describes the application of several powerful biophysical techniques to a study of intracellular signal transduction proteins. Signal transduction proteins mediate the transfer of signals from the cell surface to intracellular compartments. The process of signal transduction is crucial since it allows a cell to form a co-ordinated response to its dynamic extracellular environment serious disease may result if this process is deregulated. Therefore, with a view towards describing cellular signalling processes in both the normal and diseased conditions, the work presented in this thesis aims to generate an increased understanding of signal transduction proteins. The interactions of signal transduction proteins determine the progression of a signal along a signal transduction pathway. These biomolecular interactions between signal transduction proteins and other ligands are critically dependent on the three-dimensional structural complementarity of the interacting binding partners. The studies presented in this thesis describe investigations of the structure and function of signal transduction proteins, encompassing the characterisation of their binding partners. The investigations were performed using an array of biophysical techniques, including nuclear magnetic resonance spectroscopy, surface plasmon resonance and analytical ultracentrifugation. The results of primary importance include: (1) the identification of novel phosphoinositide binding partners for specific pleckstrin homology (PH) domains, (2) the structural characterisation of the phosphoinositide binding site on the dynamin PH domain, (3) the structural and thermodynamic characterisation of an intermolecular interaction which mediates the homodimerisation of the p85[alpha]/pll0[alpha] phosphoinositide 3-kinase, and (4) the evaluation of a recently proposed model for the role of Src homology 2 domains in the regulation of p85[alpha]/pll0[alpha] phosphoinositide 3-kinase.

Type: Thesis (Doctoral)
Qualification: Ph.D
Title: Biophysical studies of intracellular signal transduction proteins: Investigating the structure-function relationship
Open access status: An open access version is available from UCL Discovery
Language: English
Additional information: Thesis digitised by ProQuest.
Keywords: Biological sciences; Signal transduction proteins
URI: https://discovery.ucl.ac.uk/id/eprint/10098656
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