Carol Robinson grew up in Kent, England attending a local school where, in addition to her academic subjects, she learned typing, needlework and cookery. Leaving school at 16 she took up a position as a laboratory technician at Pfizer. It was here that she was first introduced to a mass spectrometer - something that was to become her vocation.
Working by day on the mass spectrometer, Carol studied before, and after, work and attended a technical college reaching degree level in seven years. In 1980 she was accepted by the University of Cambridge to continue her studies in mass spectrometry and to embark upon her doctorate. She had, by this time, left her post in Pfizer and was able to apply herself full-time to her studies, completing her PhD in just two years. Her unconventional path to PhD was to set the trend for her future career.
Early in her postdoctoral career Carol made the decision to step away from her career in order to spend time at home with her three children while they were young. During this time she took on a variety of part-time teaching posts to fit in with her family, before a chance advertisement in her local library set her back on the path to academia.
The Department of Chemistry at the University of Oxford was advertising for a postdoctoral researcher in mass spectrometry; despite her eight years away from the field, Carol decided to apply even though she knew her knowledge wouldn’t be as up to date as candidates who were actively engaged in research. Luckily, someone on the hiring committee remembered Carol from her time at Cambridge and decided to take a chance on her, and so, in early 1992 Carol re-entered academia as a postdoctoral researcher in the mass spectrometry laboratory at the University of Oxford.
Carol had a lot of catching up to do: in her time away, not only had protein chemistry advanced significantly but also computers had become an integral part of mass spectrometry. She had to learn new skills, as well as catching up with advances in her field. Not only was she soon up to speed but her research was starting to attract attention, so much so that she was able to secure a prestigious Royal Society University Research fellowship that provided her with 10 years of funding. With this funding she started to explore protein folding reactions monitoring them by mass spectrometry to provide new insight into transient states.
Continuing on this theme, in 2001 Carol returned to the University of Cambridge to continue her research into the mass spectrometry of protein assemblies and to become the first female professor in the department of chemistry. While in Cambridge she carried out her first experiments to determine the overall topology of proteins (2) and began to project intact membrane protein complexes into the gas phase (3). She returned to Oxford in 2009 to take up the Chair of Dr. Lee’s Professor of Chemistry, a position she continues to hold today. While in Oxford she has focused on the relationship between membrane proteins and lipids (4-6). With this information she is exploring new ways to characterize receptor-signaling pathways.
Despite being an accomplished leader in her field, Carol says that one of the most rewarding aspects of her job is to see young scientists in her research group going on to great positions and careers. She has always encouraged them to maintain the work – life balance. One of her own role models is Dorothy Hodgkin who succeeded in raising three children as well as having a highly distinguished scientific career.
Asked how she would describe her research to a sixth grade teacher, Carol says, “My research explores proteins and their interactions in the gas phase — an entirely new medium in which proteins can be interrogated. In this phase the protein molecules are able to express themselves in different ways. We can learn new things about the ways in which they do this. I think of it as the proteins having freedom of movement – akin to running on a track as opposed to running in a swimming pool. The protein molecules are not constrained in the gas phase as they would be in solid or liquid states.”
Carol doesn’t have any specific advice for biophysicists with children. “I am often asked if I would do the same again by women who are contemplating a career break. I don’t like to prescribe. Each situation is different and you have to do what feels right for you at the time.” She does advise, however, “Be passionate about whatever it is you do — that way you can look back without regrets.”
References
1. C. V. Robinson, M. Gross, S. J. Eyles J. J. Ewbank, M. Mayhew, F. U. Hartl, C. M. Dobson and S. E. Radford. Conformation
of GroEL-bound alpha-lactalbumin probed by mass spectrometry. Nature 372(6507): 646-651.
2. B. T. Ruotolo, K. Giles, I. Campuzano, A. M. Sandercock, R. H. Bateman and C. V. Robinson Evidence for macromolecular
protein rings in the absence of bulk water. Science 310: 1658-1661, 2005.
3. N. P. Barrera, N. Di Bartolo, P. J. Booth and C. V. Robinson. Micelles protect membrane complexes from solution to
vacuum. Science 321: 243-246, 2008.
4. M. Zhou, N. P. Morgner, A. Barrera, S. C. Politis, D. Isaacson, T. Matak-Vinkovic, R. Murata, A. Bernal, D. Stock and
C. V. Robinson. Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding.
Science 334: 380-385, 2011.
5. 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 510: 172-175, 2014.
6. K. Gupta, J. A. Donlan, J. T. Hopper, P. Uzdavinys, M. Landreh, W. B. Struwe, D. Drew, A. J. Baldwin, P. J. Stansfeld and C.
V. Robinson. The role of interfacial lipids in stabilizing membrane protein oligomers. Nature. 541: 421-424, 2017.