Interview with Dame Carol Robinson, winner of the 2022 European Chemistry Gold Medal  

The 2022 European Chemistry Gold Medal has been awarded to Professor Dame Carol Robinson for exceptional achievements in the field of chemistry in Europe. She will give the opening lecture at the 8^th European Chemistry Congress that will be held in Lisbon, Portugal, from 28 August to 1 September 2022.

Professor Dame Carol Robinson is a British chemist and former President of the Royal Society of Chemistry. She is currently the Director of the Kavli Institute for NanoScience Discovery as well as a Professorial Fellow at Exeter College and holds the Chair of Dr Lee’s Professor of Physical and Theoretical Chemistry at the University of Oxford. She is noted as the first female Professor in both the Department of Chemistry at the University of Oxford and prior to that at the University of Cambridge.

Professor Robinson’s long and distinguished career has been marked by outstanding contributions across the fields of physical, medicinal, and biochemistry; an exemplary publication record, and numerous international honours and awards for her research all whilst promoting the role of women in science.

Professor Robinson is globally recognised as a leader in the development of mass spectrometry to understand the 3D structure of large molecular compounds, specifically carrying out ground-breaking research on protein folding, ribosomes, molecular chaperones, and membrane proteins. Her cutting-edge work finds many applications from antibiotic resistance to drug design in both academia and industry. In addition to her academic role, she founded a successful biotechnology company, now in its fourth year, which focuses on mass spectrometry to discover novel medicines.

What does it mean to you to receive the European Chemistry Gold Medal?
I was absolutely delighted to win this award, particularly as it is the Society’s most prestigious medal. It is a prize that my research group shares with me and this means a lot as it is recognition of the impact of our work in the fast-moving field of mass spectrometry and membrane proteins.

How and when did you start having an interest in STEM?
I was always interested in nature as a child but in those earlier years, and at my school in particular, it was not always expected that girls would study STEM subjects in depth.  That changed for me because of one teacher – my chemistry teacher; his lessons made chemistry exciting and from then on, I was ‘hooked’.

Could you please tell us a bit about how your career has developed?
I was in a school where it was not typical for people to go on to university and so I needed to get a job when I left school.  The problem was I couldn’t yet drive and so the job needed to be local – and that’s how I came to be a technician at Pfizer after just turning 16 years old.  Very fortunately for me, one of my supervisors offered me the opportunity to gain qualifications whilst working.  This meant studying part-time over seven years before eventually graduating from the Royal Society of Chemistry.

A year later I was offered a place at Cambridge to do a PhD but it was only some ten years after this, and with an eight-year career break in-between, that my academic career really started.  This was largely due to one man – the late Professor Sir Christopher Dobson who became my lifelong friend and mentor.  I was delighted to work under Chris’ supervision as a postdoctoral fellow in Oxford.

One of the projects I was assigned was a protein folding problem.  I noticed that as the proteins were folding, they were binding to small molecules or cofactors. Everything we knew indicated this couldn’t happen in the gas phase. However, I realised it had a semblance of reality because if the proteins were not folded, the small molecules did not bind to them; only if the proteins were folded could the small molecule bind – as in nature.    This was intriguing and from then on, I knew I wanted to work with folded proteins in the gas phase – the rest is history!

You are recognised as a leader in the development of mass spectrometry to understand the 3D structure of large proteins. Could you please tell us a bit about your work?
Essentially, we develop cutting edge mass spectrometry methods to understand the structure and function of protein complexes.  We then apply this knowledge to a variety of research questions relating to health and disease.  For example, we are currently working to advance our capabilities to study membrane-embedded targets of antibacterial and antiviral agents and use this knowledge to improve their targeting.

What was the greatest challenge throughout your career as a chemist?
There have been many technical challenges: the most fundamental being the retention of the folded structure of proteins and other macromolecules in the gas phase; the most recent being developing a method to study proteins in their native membrane environments.I always knew, however, that given enough time we would somehow overcome the technical challenges. Much harder for me was gaining acceptance among my early contemporaries that my experiments had a chance of succeeding.  For a young researcher this can be daunting and a lonely path to tread; for this reason, I still consider a lack of external belief in my research one of the greatest challenges of my career.