She was a generous person and a wonderful teacher, stimulating and inspiring a generation of structural biologists in the UK and elsewhere, who will continue her philosophy of advancing science in a multidisciplinary and international context.
Source/Credit: The Guardian | UK
By Tom Blundell | October 10, 2012
Pioneering molecular biologist who shed light on how enzymes, nature's catalysts, do their work
During a special meeting at the Royal Institution in London in 1965, the first structure of an enzyme, lysozyme, was unveiled by David Phillips. The fully extended polypeptide chain hung down from the high ceiling, coming close to Phillips. In front of him was a much more compact model, defined by X-ray crystallography, of the intricately folded chain. Both represented a protein that was in real life 100m times smaller. Phillips and his colleagues identified a well-defined groove in which evolution had suggestively placed amino acid sidechains.
The most memorable part of that day was the appearance of Louise Johnson, a young graduate student, who stunned us all by describing how the enzyme bound its substrates and selectively cleaved the polysaccharide components of bacterial cell walls, giving rise to its anti-microbial properties, first described by Alexander Fleming in the 1920s. This was the birth of structural enzymology, the beginnings of a continuing investigation of the detailed structures and mechanisms of nature's catalysts.
Louise, who has died aged 71, continued to be in the vanguard of enzymology throughout her life. After completing her PhD, she moved to Yale in 1966 to work with the eminent biochemist and biophysicist Fred Richards. She returned to the UK in 1967 to rejoin Phillips, who had just been appointed to Oxford University as professor of molecular biophysics.
In Oxford she began to work on another extremely challenging project, the structure of the regulatory enzyme glycogen phosphorylase. After more than 20 years of work she was able to describe the structure of this magnificent enzyme and to explain its regulation.
Louise was born in Worcester. After attending Wimbledon high school for girls, she studied physics at University College London and then moved to the Royal Institution, where she completed her PhD in 1966. Her appointment at Oxford in 1967 was as a university demonstrator and lecturer in biophysics at Somerville College; she became a university lecturer and fellow of Somerville in 1973. On the retirement of Phillips in 1990, she was his obvious successor, becoming professor of molecular biophysics and professorial fellow at Corpus Christi College. In the same year her work was recognised by election to the Royal Society. She was made a dame in 2003.
In 1968, Louise married Abdus Salam, the brilliant Pakistani physicist and future Nobel laureate. They had two children, Umar in 1974 and Sayyeda in 1982.
I discovered Louise's grasp of physics as well as biology when Phillips asked us to write a review of protein crystallography for Biennial Reviews of Science, Technology and Medicine in July 1971, a task he had failed to start and for which the manuscript was overdue. Louise and I both sacrificed our holidays and Louise completed her sections with brilliant insights into this complex, multidisciplinary research technique. The editor accepted only our concluding section as the review and suggested we write a textbook. This we did, after negotiating a large advance with which Louise bought a horse, as one of her passions was riding. She wrote sections of the book while she was pregnant with Umar, and it was eventually published in 1976. It was reissued in 2006.
Louise's interest in physical techniques led her to accept the role of director for life sciences at the Diamond Light Source, the UK's national synchrotron science facility, in 2003. She championed advances made possible by this powerful new source of X-rays, not only in structural biology at the molecular level, but also for X-ray imaging of whole cells.
But Louise never lost her interest in understanding cell regulation through phosphorylation, including the role of protein kinases in the cell cycle. The structures she defined have provided molecular and cell biologists not only with a general model as to how the protein kinases are regulated, but also the knowledge to guide the design of cancer drugs that are now in clinical trials.
Louise had a passionate interest in science in developing countries. She played a major role as an associate member of the Third World Academy of Sciences, particularly in influencing the development of science in Islamic countries, lecturing in Iran and Pakistan, and supporting the development of Sesame, the new synchrotron in Jordan. She was a generous person and a wonderful teacher, stimulating and inspiring a generation of structural biologists in the UK and elsewhere, who will continue her philosophy of advancing science in a multidisciplinary and international context.
Abdus Salam died in 1996. Louise is survived by her children.
• Louise Napier Johnson, molecular biophysicist, born 26 September 1940; died 25 September 2012
Read original post here: Dame Louise Johnson obituary
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