Carol V. Robinson

University of Oxford


Primary Section: 21, Biochemistry
Membership Type: International Member (elected 2017)

Biosketch

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 characterize receptor-signaling complexes. Carol’s graduate education was completed whilst working full-time in industry. She was subsequently admitted to the University of Cambridge where she completed her PhD in two years. Following an eight-year career break, to begin raising her three children, she returned to research at Oxford. In 2001 she became the first female professor in Chemistry at the University of Cambridge, returning to Oxford in 2009 to take up the Chair of Dr. Lee’s Professor of Chemistry. She is President Elect of the Royal Society of Chemistry, a Fellow of the Royal Society London and a Fellow of the U.K. Academy of Medical Sciences.

Research Interests

Carol has had a long-term research interest in developing and applying mass spectrometry to structural biology. Her current recent focus is in uncovering the roles of small molecules in the structure and function of membrane proteins. To uncover these relationships she is developing a range of mass spectrometry tools that maintain protein lipid interactions as close as possible to their native bilayer environments. Using these approaches she and her team have discovered lipids that are involved in flippase reactions, in mediating drug binding and in dictating the oligomeric state of receptors and transporters. Her current research involves the study of G-protein coupled receptors and their downstream signaling partners. Capturing these receptors in the gas phase of the mass spectrometer has enabled her team to study the impact of drug binding on different kinases and on signaling cascades. Overall, therefore, her research is not only providing new insight into the role of lipids in stabilizing membrane protein complexes but is also playing an important part in drug discovery.

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