研究领域

Physical & Theoretical Chemistry

We are interested in studying the structure and dynamics of the cellular protein machinery. Through this we hope to understand the molecular basis for their function in healthy organisms, and malfunction in disease. Our research relies on combining traditional structural biology approaches with new biophysical techniques in order to interrogate our system of interest from multiple angles. In this way we can obtain a thorough description of the molecular structure and its associated dynamics.

近期论文

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Collision cross sections for structural proteomics Marklund, E.G., Degiacomi, M.T., Robinson, C.V., Baldwin, A.J., & Benesch, J.L.P. Structure (2015), in press Combining tandem mass spectrometry with ion mobility separation to determine the architecture of polydisperse proteins Shepherd, D.A., Marty, M.T., Giles, K., Baldwin, A.J., & Benesch, J.L.P. Int. J. Mass Spectrom. (2015), in press The role of the detergent micelle in preserving the structure of membrane proteins in the gas phase Reading, E., Liko, I., Allison, T.M., Benesch, J.L.P., Laganowsky, A., & Robinson, C.V. Angew. Chem. Int. Ed. (2015) in press, doi: 10.1022/anie.201411622 Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1 Brem, J., Struwe, W.B., Rydzik, A.M., Tarhonskaya, H., Pfeffer, I., Flashman, E., van Berkel, S.S., Spencer, J., Claridge, T.D.W., McDonough, M.A., Benesch, J.L.P., & Schofield, C.J. Chem. Sci. (2015), 6, 956-63 Phosphomimics destabilise HSP27 oligomeric assemblies and enhance chaperone activity Jovcevski, B., Kelly, M.A., Rote, A.P., Berg, T., Gastall, H.Y., Benesch, J.L.P., Aquilina, J.A. & Ecroyd, H. Chem. Biol. (2015), 22, 186-95 Native mass spectrometry: towards high-throughput structural proteomics Kondrat, F.D., Struwe, W.B., & Benesch, J.L.P. Methods Mol. Biol. (2014), 1261:349-71 Ejection of structural zinc leads to inhibition of γ-butyrobetaine hydroxylase Rydzik, A.M., Brem, J., Struwe, W.B., Kochan, G.T., Benesch, J.L.P., & Schofield C.J. Bioorg. Med. Chem. Lett. (2014), 24, 4954-7 Mass-selective soft-landing of protein assemblies with controlled landing energies Mikhailov, V.A. & Mize, T.H., Benesch, J.L.P., & Robinson, C.V. Anal. Chem. (2014), 86, 8321-8 Dynamical structure of αB-crystallin Hochberg, G.K.A. & Benesch, J.L.P. Prog. Biophys. Mol. Biol. (2014), 115, 11-20 The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity Hochberg, G.K.A, Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M.R., Collier, M.P., Stroud, J., Carver, J.A., Baldwin, A.J., Robinson, C.V., Eisenberg, D.S., Benesch, J.L.P. & Laganowsky, A. Proc. Natl. Acad. Sci. U.S.A. (2014), 111, E1562-70 Detergent-free mass spectrometry of membrane protein complexes Hopper, J.T., Yu, Y.T., Li, D., Raymond, A., Bostock, M., Liko, I., Mikhailov, V., Laganowsky, A., Benesch, J.L.P., Caffrey, M., Nietlispach, D., & Robinson, C.V. Nat. Methods (2013), 10, 1206-8 HSP70 oligomerization is mediated by an interaction between the interdomain linker and the substrate binding domain Aprile, F.A., Dhulesia, A., Stengel, F., Roodveldt, C., Benesch, J.L.P., Tortora, P., Robinson, C.V., Salvatella, X., Dobson, C.M., & Cremades, N. PLOS One (2013), 8, e6796 C-terminal interactions mediate the quaternary dynamics of αB-crystallin Hilton, G.R., Hochberg, G.K.A., Laganowsky, A., McGinnigle, S.I., Baldwin, A.J., & Benesch, J.L.P. Phil. Trans. Roy. Soc. B (2013), 368, 20110405 Probing dynamic conformations of the high molecular weight αB-crystallin heat shock protein ensemble by NMR spectroscopy Baldwin, A.J., Walsh, P., Hansen, D.F., Hilton, G.R., Benesch, J.L.P., Sharpe, S., & Kay, L.E. J. Am. Chem. Soc. (2012), 134, 15343-50 The unusual mycobacterial chaperonins: Evidence for in vivo oligomerization and specialization of function Fan, M., Rao, T., Zacco, E., Ahmed, M.T., Shukla, A., Ojha, A., Freeke, J., Robinson, C.V., Benesch, J.L.P., & Lund, P.A.. Mol. Micro. (2012), 85, 934-33 Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach Stengel, F., Baldwin, A.J., Bush, M.F., Hilton, G.R., Lioe, H., Basha, E., Jaya, N., Vierling, E. & Benesch, J.L.P. Chem & Biol. (2012), 19, 599-607 Small heat-shock proteins: paramedics of the cell Hilton, G.R., Lioe, H., Stengel, F., Baldwin, A.J. & Benesch, J.L.P. Top. Curr. Chem. (2012), 328, 69-98 Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionisation mass spectrometry Hilton, G.R. & Benesch, J.L.P. J. R. Soc. Interface (2012), 9, 801-16 The polydispersity of αB-crystallin is rationalised by an interconverting polyhedral architecture Baldwin A.J., Lioe, H., Hilton, G.R., Baker, L.A., Rubinstein, J.L., Kay, L.E. & Benesch, J.L.P. Structure (2011), 19, 1855-63 Mass spectrometry: come of age for structural and dynamical biology Benesch, J.L.P. & Ruotolo, B.T. Curr. Op. Struc. Biol. (2011), 21, 641-9 Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus Baldwin A.J., Hilton, G.R., Lioe, H., Bagnéris, C., Benesch, J.L.P. & Kay, L.E. J. Mol. Biol. (2011), 413, 310-20