Inaugural Louise Johnson Memorial Lecture held
Image modified from Anne-Katrin Purkiss, Wellcome Images
The Department was delighted to welcome Professor Sir Tom Blundell to give the Inaugural Louise Johnson Memorial Lecture on May 1st.
Professor Blundell from the Department of Biochemistry at the University of Cambridge spoke about ‘Genomes, Structural Biology and Drug Discovery’. Many former colleagues of Louise Johnson, who passed away in 2012, attended the event.
The lecture series has been launched to recognise and celebrate Louise Johnson’s outstanding career and achievements. The Department will host the event annually.
In his introduction, Head of Department Professor Mark Sansom said that Louise had been a wonderful mentor, colleague and role model for scientists worldwide. He added that it was fitting that Professor Blundell, a world-leading structural biologist and structural bioinformatician, should give the Inaugural Memorial Lecture.
Before presenting his own work, Professor Blundell talked about Louise, noting the similar paths that they had followed during their careers. He said that he first met Louise at the Royal Institution when she and her PhD supervisor, David Phillips, were presenting their work on the structure of lysozyme. He found her an articulate speaker and noted that she was ‘clearly doing rather better than me.’
He continued to regard Louise’s work and achievements very highly. When he moved to David Phillip’s lab in Oxford, and Louise joined, he was asked to write a review on protein crystallography with her. The comprehensive material amassed between them, considered too much for a review alone, subsequently developed into a classic textbook on the topic for students and researchers.
Professor Tom Blundell giving the Memorial Lecture
Professor Blundell said that Louise’s discoveries were crucial in laying the foundations for drug discovery. He added that whilst the structures generated by protein crystallography were beautiful in their own right, it was important to turn these into something useful and he was pleased to see the field developing in this way.
He went on to talk about his own work in which he has successfully developed new approaches to structure-guided and fragment-based drug discovery. His current interest is in the design of cancer therapeutics and new antimicrobials to fight resistance in tuberculosis. He regards tackling the disease as a priority, a view that would have resonated with Louise's interests in international scientific causes.
As one of the pioneers of modern structural biology, Louise will be remembered in particular for moving structural studies to centre stage in all areas of modern biology.
Her work has transformed our knowledge and understanding of how complex biological systems work and has uncovered fundamental biochemical mechanisms. Amongst the structures she deciphered during her career were those of lysozyme, ribonuclease S, glycogen phosphorylase and cell cycle regulatory proteins.
The determination of the structure of lysozyme when bound to N-acetyl-glucosamine, a component of bacterial cell walls which inhibits lysozyme, led to the first structural evidence that a substrate slots into an enzyme, much as a key fits into a lock.
Another highlight of her research was the determination of the structural basis of the regulation of a key enzyme, muscle glycogen phosphorylase. This work, on one of the largest and most complex proteins at the time, explained the fundamental molecular basis of protein regulation by phosphorylation.
Louise came to Oxford in 1967 where she joined David Phillips at the Laboratory of Molecular Biophysics (LMB). In 1990, she was appointed the first David Phillips Professor of Molecular Biophysics. From 2003, she combined her position at the LMB with the role of Life Sciences Director at Diamond where she continued to work after her retirement.
As well as carrying out cutting-edge research, Louise nurtured numerous careers, training a generation of crystallographers in Oxford who themselves now train future leaders across the world.