The Oxford Science Lecture Series

Professor  Carol Robinson

University of Oxford

“Finding the Right Balance”

 Dorothy Hodgkin Memorial Lecture 2014

University Museum, Oxford, 11th March 2014

The 2014 Dorothy Hodgkin Memorial Lecture was presented by Professor Dame Carol Robinson, and welcomed members of Dorothy Hodgkin’s family in the audience.

It is fifty years since Dorothy Hodgkin’s unequalled achievement of being the UK’s only woman win a Nobel Prize for Chemistry in 1964. It seems fitting, therefore, to come back to Oxford’s Department of Chemistry for this year’s speaker choice, and another woman who is making huge strides to find new ways to probe complex, 3-dimensional information about molecular structures.

The first female professor of chemistry at both Cambridge and Oxford universities, Professor Dame Carol Robinson has been a Fellow of the Royal Society of Chemistry since 2004, and has held the Doctor Lee Professor Elect at the University of Oxford since 2009. Professor Robinson has been the recipient of many awards throughout her career, among which are the Royal Society’s Rosalind Franklin Award in 2004, and the 2011 FEBS/EMBO Woman on the Year Award. In 2013, her remarkable achievements in advancing the capability of mass spectrometry as a technique to elucidate complex structural information were recognised in the New Year’s Honours list, as she became Dame Commander of the Order of the British Empire.

Professor Dame Carol Robinson opened her talk with a reminder of how little recognised women scientists still are today. A recent University Challenge episode featured a photo of Dorothy Hodgkin that went unrecognised, and when pupils were prompted in a recent study to recall Marie Curie, there was (the inevitable?) confusion with the global superstar Mariah Carey. Professor Robinson’s background featured heavily in the presentation, and the slightly unconventional path her career has taken.

Having left school at 16, Carol Robinson’s first job was as a technician at the biochemical company Pfizer. Working with mass spectrometers here set the foundations for the research she has pursued ever since. Robinson undertook undergraduate studies in chemistry at evening classes over seven years, before being accepted to study for a PhD at the University of Cambridge. Her doctoral research used mass spectrometry to piece together the sequence of units that make up the melanocyte stimulating hormone. This hormone causes fish to change colour, and was alleged to have been behind the change in Michael Jackson’s skin pigment.

Following an eight year career break, it was during a library trip with her three children that Carol found a job at Oxford University advertised in New Scientist. Working with Jack Baldwin, she developed a technique to recreate conditions found in real biological systems. In the new technique, a protein complex is suspended in a medium, and sprayed in tiny droplets, like in a sneeze. The droplets, called micelles, evaporate and shrink, until only the (intact) protein remains, flying towards a detector. Proteins that are folded to different extents appear at different positions in a mass spectrum because they carry different charges. Previous work in the area had looked at proteins in a gaseous state, but the mass spectrometry hadn’t been able to look at how proteins behave when they’re surrounded by other molecules.

Following this work, Carol applied for her own funding to design a mass spectrometer capable of measuring new, high mass ranges. In traditional spectrometers, a protein is chopped up, making a ‘proteo mix’ of component subunits. Carol believed she could design a spectrometer that would be able to measure the mass to charge ratio of intact proteins, giving information about neighbouring components. Despite being warned many times that she’d “have a short career if you do that”, Carol’s persistence resulted in a machine able to measure up to 12 million mass units, with better resolution than had been seen before. In some of the first work using the new spectrometer, a protein complex was found to be composed of two parts, one containing 14 units, and one containing seven. This was the first time 3D structural information had been found using mass spectrometry, paving the way for a powerful new tool for structural elucidation of biologically relevant molecules.

Robinson moved on to describe her work with protein complexes that are found embedded in membranes. The study of these was unpopular in mass spectrometry due to the large amount of detergent needed to solublise the complexes, which causes problems in the detector machines. The electrospray technique developed earlier in her career came into its own. When lipids attach to proteins, they can prevent the protein from folding, and this could now be monitored by mass spectrometry. Using the electrospraying ‘sneeze’ technique membrane proteins called ATP synthases, which are large molecular motors, can be released intact from detergent micelles, and their interactions with lipids (fatty acid molecules that are insoluble in water) can be studied. Another notable piece of work carried out by Robinson’s research group showed that lipid binding to the protein Aquaporin Z causes hydrophobic tryptophan arms of the molecule to unfold, opening up and making the complex float on water.

Professor Robinson reflected on her experience of a career as an academic scientist, drawing on the things that have made it particularly rewarding. Of particular importance have been having good interactions with her researchers, embracing opportunities to build friendships with colleagues, and taking up the chances to travel. She has enjoyed her career thus far. In addition, Carol feels lucky not to have missed out on family life, she’s been able to attend her children’s school sports days, and her daughter’s graduation. Carol concluded her presentation with some advice to young women entering academic careers in science.

Flexible hours and leaving at 5 p.m. should not be impossible, this may mean being available later in the evening or being able to work from home once the kids are in bed.

Carol thanked her own mentors for pushing her to go for opportunities she was hesitant about: Dudley Williams, who nominated Carol to the Royal Society; Chris Dobson, who encouraged Carol to apply for a University Research Fellowship early in her career; Professor Sunetra Gupta, Christina, and Jane who helped enormously with moving the Robinson research group to Oxford.

Take the opportunity you get to choose what is important.

And make sure you are getting something out of the collaboration.

On that note, the lecture was aptly concluded with a quote about Dorothy Hodgkin, from the Nobel Prize winning crystallographer Max Perutz:

“There was a magic about her person. She had no enemies… the warmth and gentleness of her approach to people uncovered in everyone, even the most hardened scientific crook, some hidden kernel of goodness”.

    Samantha Binding,  chemistry DPhil student,   University of Oxford.