Carol Robinson, of British nationality, is awarded the 2022 Louis-Jeantet Prize for Medicine for establishing mass spectrometry as a rigorous method to analyse the composition of protein complexes, and their interactions with small molecules.
Born in 1956, Professor Dame Carol Robinson graduated from the Royal Society of Chemistry in 1979 and completed her PhD at the University of Cambridge. She took an eight-year career break to bring up her children and later became the first female Professor of Chemistry at the University of Cambridge (2001-2009). She has held the Chair of Dr. Lee’s Professor of Chemistry at the University of Oxford since 2009 and is Oxford’s first female Professor of Chemistry. Since 2021 she has been Director of the Kavli Institute for Nanoscience Discovery.
Her work has attracted many awards including the Othmer Gold Medal from the Science History Institute, the Royal Medal A from the Royal Society, the Novozymes Prize and the Stein and Moore Award. She is the former President of the Royal Society of Chemistry, a Foreign Associate of the National Academy of Sciences USA and EMBO member. She holds fifteen honorary doctorates and offices and was appointed DBE in 2013 for her contributions to science and industry.
Soap bubbles for proteins
Carol Robinson is a founder and world leader of the native protein Mass Spectrometry (MS) field. Her focus is on membrane protein complexes and their interactions with ligands. Membrane proteins are hugely important drug targets but are incredibly hard to study as they are imbedded in a lipid hydrophobic membrane, whereas the parts on either side of the membrane are hydrophilic. When Carol Robinson began her research career, it was largely assumed that proteins needed to be denatured or even digested for analysis by MS, which entails the loss of their biological activity.
In 2008 Carol Robinson changed this perspective by discovering that intact, heterogeneous membrane protein complexes could be injected into the mass spectrometer if first imbedded in detergent micelles, or giant soap bubbles. These bubbles shield and protect the membrane proteins, so that they are transferred into the gas phase in their native folded state. Using this method, she uncovered mechanistic details of many different types of integral membrane proteins, including channels, transporters, and receptors, and has been able to study their association with lipids. Her work has wide medical impact, as her techniques are now routinely used to study a variety of processes spanning from antibody characterisation and small molecule drug screening to antibiotic resistance.
Prof. Dame Carol Robinson
Physical and Theoretical Chemistry Laboratory
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