School of Molecular and Microbial Biosciences
The University of Sydney
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Professor Jill Trewhella

Molecular and Microbial Biosciences
Faculty of Science

G08 - Biochemistry and Microbiology Building
The University of Sydney
NSW 2006 Australia

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Phone +61 2 93518782
Fax +61 2 93514726
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Research Interests

Jill Trewhella is a biophysicist who uses physical methods to study bio-molecular structures as a basis for understanding their function. A major focus of her work is on the structural biology of how bio-molecules interact and communicate in order to carry out functions that involve multiple molecular actors working in concert. This work requires a multidisciplinary approach using molecular biology, biochemistry, and biophysical tools. One frequently used biophysical tool is the small-angle scattering of x-rays and neutrons in order to probe the solution conformations of proteins and the complexes they form in a wide variety of conditions and states of activity.

Select Publications

    2009
    • Siddiqui, K, Parkin, D, Curmi, P, De Francisci, D, Poljak, A, Barrow, K, Noble, M, Trewhella, J, Cavicchioli, R. A novel approach for enhancing the catalytic efficiency of a protease at low temperature: reduction in substrate inhibition by chemical modification. Biotechnology and bioengineering. 2009; 103:676-686 [Abstract]
    • Jacques, D, Streamer, M, Rowland, S, King, G, Guss, J, Trewhella, J, Langley, D. Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state. Acta crystallographica. Section D, Biological crystallography. 2009; 65:574-581 [Abstract]
    2008
    • Jacques, D, Langley, D, Jeffries, C, Cunnigham, K, Burkholder, W, Guss, J, Trewhella, J. Histidine Kinase Regulation by a Cyclophilin-like Inhibitor. Journal of molecular biology. 2008; 384:422-35 [Abstract]
    • Whitten, A, Jeffries, C, Harris, S, Trewhella, J. Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function. Proceedings of the National Academy of Sciences of the United States of America. 2008; 105:18360-18365 [Abstract]
    • Zhan, H, Taraban, M, Trewhella, J, Swint-Kruse, L. Subdividing Repressor Function: DNA Binding Affinity, Selectivity, and Allostery Can Be Altered by Amino Acid Substitution of Nonconserved Residues in a LacI/GalR Homologue. Biochemistry. 2008; 47:8058-69 [Abstract]
    • Griffin, M, Dobson, R, Pearce, F, Antonio, L, Whitten, A, Liew, C, Mackay, J, Trewhella, J, Jameson, G, Perugini, M, Gerrard, J. Evolution of quaternary structure in a homotetrameric enzyme. Journal of molecular biology. 2008; 380:691-703 [Abstract]
    • Wang, Y, Trewhella, J, Goldenberg, D. Small-angle X-ray scattering of reduced ribonuclease A: effects of solution conditions and comparisons with a computational model of unfolded proteins. Journal of molecular biology. 2008; 377:1576-92 [Abstract]
    • Jeffries, C, Whitten, A, Harris, S, Trewhella, J. Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C. Journal of molecular biology. 2008; 377:1186-99 [Abstract]
    • Trewhella, J. The different views from small angles. Proceedings of the National Academy of Sciences of the United States of America. 2008; 105:4967-4968 [Abstract]
    • Taraban, M, Zhan, H, Whitten, A, Langley, D, Matthews, K, Swint-Kruse, L, Trewhella, J. Ligand-induced conformational changes and conformational dynamics in the solution structure of the lactose repressor protein. Journal of molecular biology. 2008; 376:466-81 [Abstract]
    • Grishaev, A, Tugarinov, V, Kay, L, Trewhella, J, Bax, A. Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. Journal of biomolecular NMR. 2008; 40:95-106 [Abstract]
    • Whitten, A, Cai, S, Trewhella, J. MULCh: modules for the analysis of small-angle neutron contrast variation data from biomolecular assemblies. Journal of Applied Crystallography. 2008; 41:222-226
    2007
    • Chan, J, Whitten, A, Jeffries, C, Bosanac, I, Mal, T, Ito, J, Porumb, H, Michikawa, T, Mikoshiba, K, Trewhella, J, Ikura, M. Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. Journal of molecular biology. 2007; 373:1269-80 [Abstract]
    • Howarth, J, Meller, J, Solaro, R, Trewhella, J, Rosevear, P. Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin. Journal of molecular biology. 2007; 373:706-22 [Abstract]
    • Comoletti, D, Grishaev, A, Whitten, A, Tsigelny, I, Taylor, P, Trewhella, J. Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering. Structure (London, England : 1993). 2007; 15:693-705 [Abstract]
    • Whitten, A, Jacques, D, Hammouda, B, Hanley, T, King, G, Guss, J, Trewhella, J, Langley, D. The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. Journal of molecular biology. 2007; 368:407-20 [Abstract]
    • Trewhella, J, Fenton, A, Thuet, K. Non-allosteric effector analogs, unique tools for identifying allosteric specific structural changes in pyruvate kinase. BIOPHYSICAL JOURNAL. 2007; 0:386A-386A [Abstract]
    • Taraban, M, Zhan, H, Matthews, K, Swint-Kruse, L, Trewhella, J. Small angle scattering studies of LacI repressor. BIOPHYSICAL JOURNAL. 2007; 0:52A-52A [Abstract]
    2006
    • Trewhella, J. Structural themes and variations in protein kinase A as seen by small-angle scattering and neutron contrast variation. European biophysics journal : EBJ. 2006; 35:585-9 [Abstract]
    • Trewhella, J. Protein kinase A targeting and activation as seen by small-angle solution scattering. European journal of cell biology. 2006; 85:655-62 [Abstract]
    • Vigil, D, Blumenthal, D, Taylor, S, Trewhella, J. Solution scattering reveals large differences in the global structures of type II protein kinase a isoforms. Journal of Molecular Biology. 2006; 357:880-889 [Abstract]
    • Trewhella, J. Neutrons reveal how nature uses structural themes and variation in biological regulation. Physica B: Condensed Matter. 2006; 385-386:825-830
    • Ramachandran, S, Trewhella, J, Tseng, Y, Yu, Y. Coassembling Peptide-Based Biomaterials: Effect of Pairing Equal and Unequal Chain Length Oligopeptides. Chemistry of Materials. 2006; 18:6157-6162