Working life: Carol Robinson
Professor Dame Carol Robinson is Professor of Chemistry at the University of Oxford. Here she tells us about her working life, from becoming fascinated with mass spectrometry to the inspirational role of mentors.
I didn’t take the conventional route to get to where I am today. I actually left school at 16, which was a common thing to do in my school at the time. I’d always been interested in chemistry, so I got a job as a lab technician at Pfizer which was my nearest pharmaceutical company.
After working on various analytical techniques, including chromatography, used to separate mixtures of substances, and nuclear magnetic resonance to determine the structure of organic compounds, I found myself in the mass spectrometry lab, which I found fascinating.
I was lucky in that my supervisors picked up on my obvious passion and fledgling ability early on. They encouraged me to take various part-time courses, which after seven years of hard work resulted in a degree and a place at Cambridge to study for a PhD.
I still feel lucky today that I get to do what I find fascinating. I’m currently using mass spectrometry ― traditionally the process used to calculate the mass of individual molecules ― to look at the structure and interaction of protein complexes, specifically membrane proteins, which regulate the transport of small molecules into and out of cells.
Understanding how proteins interact is particularly important for identifying drug targets and improving drug design. I recently used this technique to help understand how a membrane protein — an ABC transporter — exports lipids and drugs simultaneously.
The high resolution of the mass spectrometry method that we developed enabled us to detect this small molecule even though the amount of drug molecules in the pocket of the protein was only around one per cent of the total mass of the complex.
The other part of my job that I love is the people interaction and supporting members of my team in their careers. I have benefited enormously from the mentors I have had along the way, so I think it’s important for me to give something back.
One mentor was Chris Dobson, a Professor in the Department of Chemistry at the University of Cambridge, who believed in me enough to give me the opportunity to get back into research, after the eight-year career break I took to bring up my three children, by offering me a postdoc position. He always encouraged me to take up the next opportunity, the next challenge.
He knew I was ready even if I didn’t!
I’m not sure if I could pick one career highlight; I enjoy many aspects of my research and I wouldn’t like to say that one was more important.
Obviously receiving my Damehood last year (for services to science and industry) was a big honour, but so was being made a professor and receiving my first MRC fellowship… I still get a thrill each time a paper is accepted!
I greatly appreciate the flexibility that working in academia has given me. It was incredibly important to me that when the children were at school I was able to attend their parents’ evenings and sports days. And in turn, they now support me.
On one occasion, when I was appointed as a Fellow of the Royal Society (in 2004), one of my teenage sons decided he would rather go bowling but in the end he came to the ceremony. All three came to watch me receive my Damehood despite the fact that they now live all over the world. When my son, now 30, spread the news of my Damehood on Facebook I knew that I had made it in his eyes!
Academia has allowed me to follow my instincts, even if something doesn’t seem right at first or is a bit risky. That was actually how I came to study protein complexes. I was originally looking at protein folding pathways, but then I noticed that some of the complexes were maintained in the gas phase of the mass spectrometer. At first I didn’t believe this, but I started studying these complexes and found I could rationalise them, despite it being a controversial area of research at the time.
My favourite response to the question, “Has it worked?” is “Not yet.” If you’ve got a good idea, believe in yourself and believe that it is going to work.
One of my most thrilling moments of discovery was seeing the first really large protein complex ‘fly’ through the mass spectrometer. And more recently, discovering how membrane proteins bind to lipids, which then changes their structure and function.
This exciting discovery will further our knowledge of the role of lipids in drug binding and therefore, I believe, lead to better drug design in the future.
As told to Ellen Charman
A version of this article was originally published in the Autumn 2014 edition of Network.