Speaker: Prof. Jill Trewhella, University of Sydney, Sydney, Australia.

Date: 2010-10-29

Time: 14:15 - 15:15

Place: Chemistry Department, Lecture Hall C, Getingevägen 60, 222 41 LUND.

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About the speaker: Professor Jill Trewhella is Professor of Molecular and Microbial Biosciences at the University of Sydney with a joint appointment in the Bragg Institute. She received her BSc (Hons 1) in Physics and Applied Mathematics (1975) and MSc in Physics (1978) from the University of New South Wales. Her PhD (1981) is in Chemistry from the University of Sydney. She moved to the United States in 1980 to complete post doctoral studies at Yale University in the Department of Biophysics and Biochemistry, and in 1984 went to Los Alamos National Laboratory to establish a structural molecular biology program associated with the spallation neutron source there. Jill held various science leadership and management positions at Los Alamos before being named Laboratory Fellow (1995) in recognition of sustained outstanding contributions to science and technology. She has published ~100 original research papers, book chapters, pedagogical articles, and reviews on structural biology, with a focus on molecular signaling in cells and the control of enzyme activity. This work gained her the recognition of being named a Fellow of the American Association for the Advancement of Science and a 2004 Australian Federation Fellow.

Abstract: The small-angle scattering from macromolecules in solution yields low-resolution structural information that complements higher resolution information from crystallography and NMR. The ever increasing desire to understand more complex and often dynamic bio-molecular systems, has brought about a surge in interest in the technique, greatly facilitated by recent developments in sources, instrumentation, and the availability of 3D modelling capabilities.  Modelling 3D structures from solution scattering data does not always lead to a uniquely determined solution, and there are inherent limits to the information content of a scattering profile beyond the issue of resolution. The inclusion of neutron scattering data with contrast variation can increase the information content, especially for bio-molecular complexes with components having distinct scattering densities. We study the protein complexes involved in signalling and regulation using a combination of small-angle X-ray and neutron solution scattering data with crystallographic and NMR results. Our specific interests include the regulatory mechanisms controlling bacterial responses to environmental signals [1] and the actions of heart muscle proteins [2]. In parallel we have been developing methods to improve the accuracy of solution structural analysis of individual protein structure by co-refinement of NMR and small-angle X-ray scattering data [3]. This presentation with describe the strengths and limitations of these approaches in the context of understanding bio-molecular function.    

1. Whitten, A. E, Jeffries, C. M., Harris, S. P., and Trewhella, J. "Cardiac myosin binding protein-C decorates F-actin: Implications for cardiac function," Proc. Natl Acad. Sci. U.S.A. 105, 18360-18365, 2008.
2. Jacques, D. A., Langley, D. B., Jeffries, C. M., Cunningham, K. A., Burkholder, W. F., Guss, J. M., and Trewhella, J. "Histidine Kinase Inhibition by a Cyclophilin-like Inhibitor," J. Mol. Biol. 384, 422-435, 2008.  
3. Grishaev, A., Tugarinov, V., Kay, L. E., Trewhella, J., and Bax, A. (2008) J. Biomol. NMR 40, 95-106.

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