Professor Dame Carol Robinson, FRS

Doctor of Science Professor Dame Carol Robinson

Tuesday 15 July 2013 at 2.30 pm - Orator: Professor Paula Booth

Mr Vice- Chancellor,

Professor Dame Carol Robinson is an exceptional scientist. Galileo counselled “measure what is measureable, and make measurable what is not so”. Carol has made the immeasurable, measurable and in doing so she has pioneered a new field of research.

Whilst many may be watching their weight, Carol’s interest in weight is quite different. She is interested in weighing proteins. Proteins are the worker molecules in living organisms, where they perform an astounding array of functions necessary to keep us alive. Many of these functions arise from carefully orchestrated interactions of several proteins in complex structures. However, such large structures have been notoriously difficult to measure. Through ground-breaking studies employing mass spectrometry, Carol has evaluated some of the most elusive protein complexes. By determining the mass of these large complexes and their constituent building blocks, Carol has elucidated the protein architectures. Her flair for mass spectrometry enabled Carol to conceive an instrument for the study of very large structures. Although this new type of instrument is now present in many laboratories throughout the world, Carol’s ability to constantly innovate and design her own machines, means that she is always a step ahead. Her laboratory contains unique, state-of the-art spectrometers and most of her work is unmatched in the world.

In order to perform these protein mass measurements, Carol had to fly the protein structures through a gas. Although this had been achieved for individual proteins, it was deemed more or less impossible to fly intact, large complexes. Carol, however, was undaunted and, much like Airbus with the 380 super jumbos, she was able to get some implausible shapes airborne. Not only did she overcome the barriers of scientific dogma, but also those of Nature. Some of her most impressive work involves protein complexes in the membrane boundary of the cells in living organisms. This membrane provides a barrier between the cell interior and the outside world, with membrane protein complexes providing tightly regulated entry points to the cell. Carol had to devise yet more new methods to fly these proteins, because their natural membrane location excludes water. This was a problem because all existing approaches were designed around proteins that reside in aqueous environments. Carol’s success with membrane proteins represents a new era. Her advances will aid drug discovery by enabling greater insight into the numerous membrane proteins that are the targets of medicines.

Carol has received numerous accolades for her seminal research. In 2004 she was elected a Fellow of the Royal Society. Earlier this year she was appointed Dame Commander of the Order of the British Empire for her services to science and industry.

Carol has also been a pioneer in other areas of science and academia. Upon her appointment in 2001, she became the first female Professor of Chemistry at the University of Cambridge. The University of Oxford had to wait a little longer, until Carol moved her laboratory there in 2009, when she became the first female Professor of Chemistry at that University. This male-domination of science and Chemistry is by no means uncommon, but Carol has made a difference as an outstanding scientist who challenges convention. She is renowned for her mentoring and support of women, and for creating a highly successful, but supportive and flexible working environment. Carol may throw the weight of a protein around, but not her own. Throughout her career she has remained gracious and modest, despite the somewhat forceful attitudes she has had to deal with, when oft being deemed not part of the club. Carol will leave her mark, not only because of her scientific achievements but also because she has altered perception. In the words of Coco Chanel: “fashion changes, but style endures”.

In keeping with Carol’s individuality, her own career path goes against the norm. She left school after her O levels to work as a technician at Pfizer, cutting her teeth in mass spectrometry, as well as studying part-time for her national certificate and degree. Her talent and tenacity were obvious and she went on to complete her PhD in 2 years at the University of Cambridge, rather than taking the more usual 3 to 4 years. She was then awarded a Training Fellowship from the Medical Research Council to work here, at the University of Bristol, with Professor Peter Bennett in the Department of Pathology and Microbiology. Carol was learning genetic engineering and bacteriology at the time, which involved using quite a lot of radioactivity. This caused her some concern as she was expecting her first child, but thanks to her care and attention her son turned out fine. What made a lasting impression, however, was staggering up the hill, pregnant, to work everyday. Subsequently, Carol took a career break of 8 years to spend time with her 3 children, and perhaps to avoid the hills of Bristol. Although, even now it is seen as near impossible to return to academic science after such a long break, Carol proved this notion foolish some years ago, and came back with a vengeance. She returned to a post-doctoral position and then a prestigious Royal Society University Research Fellowship at the University of Oxford. It was during this time that she began to show her prowess in protein mass spectrometry. Within 10 years of her return to science, Carol was making history as the first female Chemistry Professor at Cambridge.

Carol is worth her weight in gold. She is outstanding and inspirational, and has had the courage to step outside convention. To our graduates today, her career shows that you do not have to kowtow to societal pressures or the expectations of others. But, instead, forge your own path by following your own convictions.

Mr Vice-Chancellor, I present to you Carol Vivien Robinson as eminently worthy of the degree of Doctor of Science honoris causa.


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