Carol V. Robinson
Carol Vivien Bradley
10 April 1956
|Thesis||Structural studies on bioactive organic compounds (1982)|
Dame Carol Vivien Robinson,(née Bradley, born 10 April 1956 ) is a British chemist and former President of the Royal Society of Chemistry (2018 - 2020). She is a Royal Society Research Professor at the Physical and Theoretical Chemistry Laboratory at the University of Oxford, as well as the Dr Lee's Professor of Physical and Theoretical Chemistry, and a Professorial Fellow at Exeter College. She was previously Professor of Mass Spectrometry at the Department of Chemistry of the University of Cambridge.
Born in Kent, the daughter of Denis E. Bradley and Lillian (née Holder),Carol Vivien Bradley left school at 16 and began her career as a lab technician in Sandwich, Kent with Pfizer, where she began working with the then novel technique of mass spectrometry.
Her potential was spotted, and she gained further qualifications at evening classes and day release from her job at Pfizer. After earning her degree, she left Pfizer and studied for a Master of Science degree at the University of Swansea, followed by a PhD at the University of Cambridge,which she completed in just two years, rather than the more usual three. During this time she was a student at Churchill College, Cambridge.
After a postdoctoral training fellowship at the University of Bristol,Robinson took up a junior position in the mass spectrometry unit at the University of Oxford, where she began analysing protein folding. Robinson and colleagues successfully captured protein folding in the presence of the chaperone GroEL, demonstrating that at least some aspects of protein secondary structure could be studied in the gas phase.
Robinson has broken ground as the first female professor in the department of chemistry at both the University of Cambridge (2001) and the University of Oxford (2009).Her research has pushed the limits of electrospray ionization mass spectrometry, demonstrating that proteins and other complex macromolecules can be studied in the gas phase. In addition to her contributions to the study of protein folding, Robinson has conducted important work on ribosomes, molecular chaperones and most recently membrane proteins. Her research has made seminal contributions to gas-phase structural biology, with progress toward the study of protein complexes in their native environments for drug discovery. Additionally, she is Co-founder and director of OMass Therapeutics, a University of Oxford spin-out company applying mass spectrometry technology to drug discovery.
Robinson was awarded the American Society for Mass Spectrometry's Biemann Medal in 2003, and the Christian B. Anfinsen Award in 2008. In 2004 the Royal Society awarded her both a Fellowship (FRS)and the Rosalind Franklin Award. Her nomination for the Royal Society reads:
Distinguished for her research on the application of mass spectrometry to problems in chemical biology. She has used mass spectrometry to define the folding and binding of interacting proteins in large complexes. Most importantly, she has established that macromolecular complexes such as GroEL, ribosomes, and intact virus capsids can be generated in the gas phase and their electrospray mass spectra recorded. This work has demonstrated the power of mass spectrometry in studying very large complexes and allowed her to define changes in their conformation and the manner of their assembly.
In 2010 Robinson received the Davy Medal "for her ground-breaking and novel use of mass spectrometry for the characterisation of large protein complexes".
In 2011 she was given the Interdisciplinary Prize by the Royal Society of Chemistry for "development of a new area of research, gas-phase structural biology, using highly refined mass spectrometry techniques",the Aston Medal, and the FEBS/EMBO Women in Science Award.
She has been awarded honorary doctorates from the University of Kent, the University of York, and the University of Bristol.
She was appointed Dame Commander of the Order of the British Empire (DBE) in the 2013 New Year Honours for services to science and industry.
She received the Thomson Medal Award in 2014.
In 2015 she was a laureate of the L'Oréal-UNESCO For Women in Science Awards; "For her groundbreaking work in macromolecular mass spectrometry and pioneering gas phase structural biology by probing the structure and reactivity of single proteins and protein complexes, including membrane proteins."She was also made a Rhodes Trustee.
In 2017 she was elected a Foreign Associate of the US National Academy of Sciences.
In 2018 she won the Frank H. Field and Joe L. Franklin Award for Outstanding Achievement in Mass Spectrometry from the American Chemical Society.
In 2019 she won the Novozymes Prize for "almost single-handedly founding a subfield of mass spectrometry proteomics".Also in 2019 she received the Royal Medal.
In 2020, she was chosen as the recipient of the Othmer Gold Medal.
Susan Lee Lindquist, ForMemRS was an American professor of biology at MIT specializing in molecular biology, particularly the protein folding problem within a family of molecules known as heat-shock proteins, and prions. Lindquist was a member and former director of the Whitehead Institute and was awarded the National Medal of Science in 2010.
Mass spectrometry (MS) is an analytical technique that is used to measure the mass-to-charge ratio of ions. The results are typically presented as a mass spectrum, a plot of intensity as a function of the mass-to-charge ratio. Mass spectrometry is used in many different fields and is applied to pure samples as well as complex mixtures.
Electrospray ionization (ESI) is a technique used in mass spectrometry to produce ions using an electrospray in which a high voltage is applied to a liquid to create an aerosol. It is especially useful in producing ions from macromolecules because it overcomes the propensity of these molecules to fragment when ionized. ESI is different from other ionization processes since it may produce multiple-charged ions, effectively extending the mass range of the analyser to accommodate the kDa-MDa orders of magnitude observed in proteins and their associated polypeptide fragments.
Tandem mass spectrometry, also known as MS/MS or MS2, is a technique in instrumental analysis where two or more mass analyzers are coupled together using an additional reaction step to increase their abilities to analyse chemical samples. A common use of tandem MS is the analysis of biomolecules, such as proteins and peptides.
Anthony James Pawson, was a British-born Canadian scientist whose research revolutionised the understanding of signal transduction, the molecular mechanisms by which cells respond to external cues, and how they communicate with each other. He identified the phosphotyrosine-binding Src homology 2 as the prototypic non-catalytic interaction module. SH2 domains serve as a model for a large family of protein modules that act together to control many aspects of cellular signalling. Since the discovery of SH2 domains, hundreds of different modules have been identified in many proteins.
Richard Neil Zare is the Marguerite Blake Wilbur Professor in Natural Science and a Professor of Chemistry at Stanford University. Throughout his career, Zare has made a considerable impact in physical chemistry and analytical chemistry, particularly through the development of laser-induced fluorescence (LIF) and the study of chemical reactions at the molecular and nanoscale level. LIF is an extremely sensitive technique with applications ranging from analytical chemistry and molecular biology to astrophysics. One of its applications was the sequencing of the human genome.
Rudolf Aebersold is a Swiss biologist, regarded as a pioneer in the fields of proteomics and systems biology. He has primarily researched techniques for measuring proteins in complex samples, in many cases via mass spectrometry. Ruedi Aebersold is a professor of Systems biology at the Institute of Molecular Systems Biology (IMSB) in ETH Zurich. He was one of the founders of the Institute for Systems Biology in Seattle, Washington, where he previously had a research group.
Dame Janet Maureen Thornton, is a senior scientist and director emeritus at the European Bioinformatics Institute (EBI), part of the European Molecular Biology Laboratory (EMBL). She is one of the world's leading researchers in structural bioinformatics, using computational methods to understand protein structure and function. She was formerly director of the EBI from October 2001 to June 2015, and played a key role in ELIXIR.
Desorption electrospray ionization (DESI) is an ambient ionization technique that can be coupled to mass spectrometry for chemical analysis of samples at atmospheric conditions. Coupled Ionization sources-MS systems are popular in chemical analysis because the individual capabilities of various sources combined with different MS systems allow for chemical determinations of samples. DESI employs a fast-moving charged solvent stream, at an angle relative to the sample surface, to extract analytes from the surfaces and propel the secondary ions toward the mass analyzer. This tandem technique can be used to analyze forensics analyses, pharmaceuticals, plant tissues, fruits, intact biological tissues, enzyme-substrate complexes, metabolites and polymers. Therefore, DESI-MS may be applied in a wide variety of sectors including food and drug administration, pharmaceuticals, environmental monitoring, and biotechnology.
David E. Clemmer is an analytical chemist and the Distinguished Professor and Robert and Marjorie Mann Chair of Chemistry at Indiana University in Bloomington, Indiana, where he leads the Clemmer Group. Clemmer develops new scientific instruments for ion mobility mass spectrometry (IMS/MS), including the first instrument for nested ion-mobility time-of-flight mass spectrometry. He has received a number of awards, including the Biemann Medal in 2006 "for his pioneering contributions to the integration of ion mobility separations with a variety of mass spectrometry technologies."
John R. Yates III is an American chemist and professor of chemical biology at The Scripps Research Institute in La Jolla, California. His work is focused on developing tools and in proteomics and he specializes in mass spectrometry. He is best known for the development of the SEQUEST algorithm for automated peptide sequencing and Multidimensional Protein Identification Technology (MudPIT).
Dame Henrietta Miriam Ottoline Leyser is a British plant biologist and Regius Professor of Botany at the University of Cambridge, Chief Executive Officer of UK Research and Innovation (UKRI) and the Sainsbury Laboratory, Cambridge.
Dame Caroline Dean is a British plant scientist working at the John Innes Centre. She is focused on understanding the molecular controls used by plants to seasonally judge when to flower. She is specifically interested in vernalisation — the acceleration of flowering in plants by exposure to periods of prolonged cold. She has also been on the Life Sciences jury for the Infosys Prize from 2018.
Albert J.R. Heck is a Dutch scientist and professor at Utrecht University, the Netherlands in the field of mass spectrometry and proteomics. He is known for his work on technologies to study proteins in their natural environment, with the aim to understand their biological function. Albert Heck was awarded the Spinoza Prize in 2017, the highest scientific award in the Netherlands.
Catherine Clarke Fenselau is an American scientist who was the first trained mass spectrometrist on the faculty of an American medical school; she joined Johns Hopkins School of Medicine in 1968. She specializes in biomedical applications of mass spectrometry. She has been recognized as an outstanding scientist in the field of bioanalytical chemistry because of her work using mass spectrometry to study biomolecules.
Sheena Elizabeth Radford FRS FMedSci is a British biophysicist, and Astbury Professor of Biophysics in the Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology at the University of Leeds. Radford is the Associate Editor of the Journal of Molecular Biology.
G. Marius Clore MAE, FRSC, FRS is a British-born, American molecular biophysicist and structural biologist. He was born in London, U.K. (1955) and is a dual US/U.K. Citizen. He is a Member of the National Academy of Sciences, a Fellow of the Royal Society, a NIH Distinguished Investigator, and the Chief of the Molecular and Structural Biophysics Section in the Laboratory of Chemical Physics of the National Institute of Diabetes and Digestive and Kidney Diseases at the U.S. National Institutes of Health. He is known for his foundational work in three-dimensional protein and nucleic acid structure determination by biomolecular NMR spectroscopy, for advancing experimental approaches to the study of large macromolecules and their complexes by NMR, and for developing NMR-based methods to study rare conformational states in protein-nucleic acid and protein-protein recognition. Clore's discovery of previously undetectable, functionally significant, rare transient states of macromolecules has yielded fundamental new insights into the mechanisms of important biological processes, and in particular the significance of weak interactions and the mechanisms whereby the opposing constraints of speed and specificity are optimized. Further, Clore's work opens up a new era of pharmacology and drug design as it is now possible to target structures and conformations that have been heretofore unseen.
Sarah Amalia Teichmann is head of cellular genetics at the Wellcome Sanger Institute and a visiting research group leader at the European Bioinformatics Institute (EMBL-EBI). She serves as director of research in the Cavendish Laboratory, at the University of Cambridge and a senior research fellow at Churchill College, Cambridge.
The Biemann Medal is awarded annually by the American Society for Mass Spectrometry (ASMS) to an individual early in his or her career in recognition of significant achievement in basic or applied mass spectrometry. It is named after professor Klaus Biemann.
Claire Eyers is a British biological mass spectrometrist who is professor of biological mass spectrometry at the University of Liverpool, where she heads up the Centre for Proteome Research. Her research publications list her either as Claire E Haydon or Claire E Eyers.