Professor Dame Carol Robinson



  • Senior Fellow
  • Molecular Architecture of Life


  • University of Oxford
Physical & Theoretical Chemistry


  • United Kingdom


Graduate of Royal Society of Chemistry
PhD, University of Cambridge


Carol holds the Chair of Dr. Lee’s Professor of Chemistry at the University of Oxford.  She is recognised for using mass spectrometry to further research into the 3D structure of proteins and their complexes.  

During her early research Carol developed and applied mass spectrometry to show how protein folding could be monitored in the presence of molecular chaperones. This research prompted her to find new ways to preserve mega Dalton complexes in the gas phase and led her to uncover the heterogeneity and dynamics of numerous multi protein complexes. In recent work she demonstrated the numerous roles played by lipids in regulating the structure and function of membrane protein assemblies.  Her current interest is in uncovering the synergy of lipid and drug binding. With this information she is exploring new ways to characterise receptor-signalling complexes. Carol’s team comprises researchers with diverse backgrounds: from chemists and physicists to structural biologists and engineers, they all work towards the common goal of deciphering protein structure and function in the gas phase.


President of the Royal Society of Chemistry, 2018

American Chemical Society, Field and Franklin Award, 2018

Foreign Associate of the US National Academy of Sciences, 2017

Dame Commander of the Order of the British Empire, 2013

Relevant Publications

H-Y Yen, K. K. Hoi, I. Liko, G. Hedger, M. R. Horrell, W. Song, D. Wu, P. Heine, T. Warne, Y. Lee, B. Carpenter, A. Plückthun, C. G. Tate, M. S. P. Sansom and C. V. Robinson. PtdIns(4,5)P2 stabilizes active states of GPCRs and enhances selectivity of G-protein coupling. Nature, 2018 559(7714): 423–427

K. Gupta, J. Li, I. Liko, J. Gault, C. Bechara, D. Wu, J. T. S. Hopper, K. Giles, J. L. P. Benesch and C. V. Robinson. Identifying key membrane protein lipid interactions using mass spectrometry. Nat Protoc, 2018, (5): 1106-1120

K. Gupta, J. A. Donlan, J. T. Hopper, P. Uzdavinys, M. Landreh, W. B.Struwe, D. Drew, A. J. Baldwin, P.J. Stansfeld, C.V. Robinson. The role of interfacial lipids in stabilizing membrane protein oligomers. Nature, 2017, 541: 421-424

I. Liko, M. T. Degiacomi, S. Lee, T. D. Newport, J. Gault, E. Reading, J. T. S. Hopper, N. G. Housden, P. White, M. Colledge, A. Sula, B. A. Wallace, C. Kleanthous, P. J. Stansfeld, H. Bayley, J. L. P. Benesch, T. M. Allison and C. V. Robinson Lipid binding attenuates channel closure of the outer membrane protein OmpF. Proc Natl Acad Sci USA, 2018, 115(26):6691-6696

A. Laganowsky, E. Reading, T. M. Allison, M. B. Ulmschneider, M. T. Degiacomi, A. J. Baldwin and C. V. Robinson Membrane proteins bind lipids selectively to modulate their structure and function. Nature, 2014, 510(7503), 172-175


Robinson Lab