Justin Benesch

Tutorial Fellow in Physical Chemistry; Professor of Biophysical Chemistry

Teaching

Teaching experience including lecturing undergraduates and graduates in biophysics and physical chemistry, tutoring in undergraduate physical chemistry, coordinating seminar series for PhD students, and outreach teaching in schools in the UK and developing world.

Research

Justin’s research has garnered an international reputation for innovative biophysical chemistry approaches based on combining mass measurement with other experimental methods, simulations, and quantitative thermodynamic and kinetic analyses. This has allowed him and his group to change our thinking as to how proteins assemble, interact, and even evolve.

After a degree in Chemistry at the University of Oxford, Justin obtained his PhD from the University of Cambridge for the development and application of novel mass spectrometry approaches. He was awarded fellowships from the Medical Research Council and Royal Society, and appointed to faculty at the University of Oxford in 2012 as an Associate Professor in Biophysical Chemistry, and Tutorial Fellow in Physical Chemistry at University College. Justin has been recognised by the Cell Stress Society International with the Alfred Tissières Award, the Howard Prize Lecture from the Biophysical Sciences Institute at Durham, and the Norman Heatley Award from the Royal Society of Chemistry in 2019.

His group’s research impacts broadly the interface between chemistry and the life sciences. Their insights have been important to understanding molecular chaperone (mal)function in humans, and the stress tolerance of plants; and their innovations in mass measurement approaches have provided new means for researchers to quantify biomolecules and their interactions.

Selected Publications

• Collier, M.P., Alderson, T.R., de Villiers, C.P., Nicholls, D., Gastall, H.Y, Allison, T.M., Degiacomi, M.T., Fuerst, D.O., van de Ven, P.F.M., Djinovic-Carugo, K., Baldwin, A., Watkins, H., Gehmlich, K., Benesch, J.L.P. “HSPB1 phosphorylation regulates its intramolecular dynamics and mechanosensitive molecular chaperone interaction with filamin C” – Science Advances, (2019), 5, eaav8421
• Malay, A.D., Miyazaki, N., Biela, A., Chakraborti, S., Majsterkiewicz, K., Stupka, I., Kaplan, C.S., Kowalczyk, A., Piette, B.M.A.G., Hochberg, G.K.A., Wu, D., Wrobel, T.P., Fineberg, A., Kushwah, M.S., Kelemen, M., Vavpetič, P., Pelicon, P., Kukura, P., Benesch, J.L.P., Iwasaki, K., Heddle, J.G. “An ultra-stable gold-coordinated protein cage displaying reversible assembly” – Nature, (2019), 569, 438-42
• Alderson, T.R., Roche, J., Gastall, H.Y., Pritišanac, I., Ying, J., Bax, A., Benesch, J.L.P.*, Baldwin, A.J. “Local unfolding of the HSP27 monomer regulates chaperone activity” – Nature Communications (2019), 10, 1068
• Lyon, Y.A., Collier, M.P., Riggs, D.L., Degiacomi, M.T., Benesch, J.L.P.*, Julian, R. “Structural and functional consequences of age-related isomerization in α-crystallins” Journal of Biological Chemistry, (2019), 294, 7546-55, and bioRxiv 364497; doi:10.1101/364497
• Young, G., Hundt, N., Cole, D., Fineberg, A., Andrecka, J., Tyler, A., Olerinyova, A., Ansari, A., Marklund, E.G., Collier, M.P., Chandler, S.A., Tkachenko, O., Allen, J., Crispin, M., Billington, N., Takagi, Y., Sellers, J.R., Eichmann, C., Selenko, P., Frey, L., Riek, R., Galpin, M.R., Struwe, W.B., Benesch, J.L.P.*, Kukura, P. “Quantitative mass imaging of single biological macromolecules” – Science (2018) 360 (6387), 423-427
• Hochberg, G.K.A., Shepherd, D.A., Marklund, E.G., Santhanagoplan, I., Degiacomi, M.T., Laganowsky, A., Allison, T.M., Basha, E., Marty, M.T., Galpin, M.R., Struwe, W.B., Baldwin, A.J., Vierling, E., Benesch, J.L.P. “Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions” – Science (2018), 359, 930-5
• Hilton, G. R., Hochberg, G., Laganowsky, A., McGinnigle, S. I., Baldwin, A.J., Benesch, J.L.P “C-terminal interactions mediate the quaternary dynamics of αB-Crystallin ” – Philosophical Transactions of the Royal Society B, (2013), 368, 20110405
• Stengel, F., Baldwin, A.J., Bush, M.F., Hilton, G.R., Lioe, H., Basha, E., Jaya, N., Vierling, E., Benesch, J.L.P. “Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach” – Chemistry & Biology, (2012), 19, 599-607
• Baldwin, A.J., Lioe, H., Hilton, G., Bagnéris, C., Baker, L.A., Rubinstein, J.L., Kay, L.E., Benesch, J.L.P. “The polydispersity of αB-crystallin is rationalized by an inter-converting polyhedral architecture” – Structure (2011), 19, 1855-63
• Stengel, F., Baldwin, A.J., Painter, A.J., Jaya, N., Basha, E., Kay, L.E., Vierling, E., Robinson, C.V., Benesch, J.L.P. “Quaternary dynamics and plasticity underlie small heat shock protein chaperone function” – Proceedings of the National Academy of Sciences USA (2010) 107, 2007-12