7 March 2014

Using Nuclear Magnetic Resonance (NMR) to Study Protein Function in Cancer and Infection

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SCI's Biotechnology Group in conjunction with the University of Westminster

University of Westminster, 115 New Cavendish Street, London W1W 6UW

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Protein NMR spectroscopy allows the determination of protein structure, dynamics and interactions with ligands or other proteins. This talk describes pieces of work underway in Dr Blumenschein´s research group at the University of East Anglia, applying protein NMR to different problems. ADAM-15 is a transmembrane protein with a large extracellular domain and a small intracellular domain, subject to alternative splicing. Different isoforms of the cytoplasmic domain are associated with different prognosis in breast cancer, and this is believe to be due to different interactions with SH3 domains of signalling kinases. We are using NMR to look at how the different isoforms interact with the kinases. Tarp (translocated actin recruiting protein) is an intrinsically disordered protein from Chlamydia involved in host cell invasion. In the initial stages of infection, the effector Tarp is injected into the host cell, where it nucleates the formation of actin filaments. Using NMR and other biophysical techniques, we have been looking at the interaction between Tarp and actin, and how Tarp changes its secondary structure upon binding. The last example is Avr3a11, an effector from a plant pathogen, Phytophthora capsicii. We have used NMR to determine the solution structure of the effector domain from Avr3a11 and study its dynamics.
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University of Westminster

University of Westminster, School of Life Sciences, 115 New Cavendish Street London W1W 6UW


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+44 (0)20 7598 1561

Email: Communications@soci.org


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Additional Info


Dr Tharin Blumenschein, Lecturer in Biomolecular NMR, School of Chemistry, Faculty of Science, University of East Anglia