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. Read more
Dr Richard Coward is an MRC Senior Clinical Fellow and Head of Research for the School of Clinical Sciences at the University of Bristol. Here he tell us about his working life from spending time with ‘beautiful’ cells to working with the pharmaceutical industry.
My MRC Senior Clinical Scientist Fellowship enables me to combine clinical and basic scientific work, allowing me to continue my laboratory and research interests as well as my clinical commitment to paediatric nephrology.
I was attracted to research at the end of my clinical training. The drive to do this was because I looked after a patient who had an inherited condition called congenital nephrotic syndrome, a disorder passed down through families in which a baby develops massive amounts of protein in the urine.
Soon afterwards it became clear that the podocyte cell, a beautiful cell in the glomerulus ― the filtering unit of the kidney ― that looks like a big octopus, was involved. The gene responsible for the disorder was discovered to code for a protein located exclusively in the podocyte. Read more
Dr Lori Passmore is head of the Mechanisms of Macromolecular Machines group in the Structural Studies Division at the MRC Laboratory of Molecular Biology (LMB). She showed Isabel Baker around her shiny new office where she approaches biological questions using structural biology methods.
These coasters were made by a friend of mine who does glass fusing. She’s put some actual electron microscopy (EM) grids, which we use to image proteins, inside the glass. Each grid is 3mm in diameter, made of a disc of metal such as copper or gold, often with a layer of carbon on top. To use these grids in the lab, we pipette a few microlitres of protein in solution on top and remove the excess solution, leaving a thin layer containing the protein. For cryo-EM – where we freeze the samples at liquid nitrogen temperature to preserve them in the vacuum of the microscope – the carbon has holes in it. When you freeze the grid, the protein molecules are trapped in ice suspended across the holes. We then image the protein, in the suspension of ice across the grid. Read more