After her PhD, she moved to the laboratory of Frederic M. Richards at Yale University for postdoctoral research in 1966. At Yale she worked as part of a team with Frederic M. Richards and Hal Wyckoff on the crystal structure of another enzyme, ribonuclease, which was solved shortly after she left: the fourth protein structure solved. After her post-doctoral year at Yale, she returned to the UK in 1967 and took up the post of Departmental Demonstrator in the Department of Zoology, University of Oxford.
By 1968, this love affair was in full swing, and secretly. However, Dr. Abdus Salam was still married to Amtul Hafeez (she died in 2007, his first-cousin), she was the sister of Col. G.M. Iqbal. Allegedly, Salam and Louise Johnson were married in a Qadiani wedding in London in 1968. An unlikely witness was Paul Mathews, Salam’s long-time research partner and professor at Imperial (See Fraser, “Cosmic Anger”, page 230-231).
Her son was born in 1974 (Umar) and a daughter was born in 1982 (Saeeda). Both of these children are shunned by the Ahmadiyya Movement. In 1973 she was appointed University Lecturer, a post which was associated with Somerville College, Oxford. She became an Additional Fellow of the college and the Janet Vaughan Lecturer. She was now able to expand her team of graduate students and post-doctoral researchers. The phosphorylase work developed and by 1978 the team had discovered its structure and were able to work on its biological control properties.
She was David Phillips Professor of Molecular Biophysics at the University of Oxford from 1990 to 2007, and later an emeritus professor.
Louise Johnson was born on 26 September 1940 in Worcester, the second of the three daughters of George Edmund Johnson (1904–1992), a former wool broker then serving in the RAF (in which he reached the rank of Wing Commander), and his wife Elizabeth Minna, née King (1914–1992). The family moved around the country following George Johnson’s RAF postings, from Exton to Market Harborough, and then to London in 1946. Louise attended Putney High School and then a school in Aberdeen, where the family lived for three years in the early 1950s, before moving to Wimbledon High School for Girls on their return to London. There she excelled, eventually becoming head girl. Her headmistress was an important inspiration to her. Both her school and family put a great value on girls’ education. Her mother had obtained a degree from University College London (UCL), and it was at the same institution that Louise studied for a BSc degree in physics, graduating in 1962.
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1952-1959 https://en.wikipedia.org/wiki/Louise_Johnson
Johnson attended Wimbledon High School for Girls from 1952 to 1959, where girls were encouraged to study science and to pursue useful careers. ______________________________________________________________________________________________
1959 https://en.wikipedia.org/wiki/Louise_Johnson
Her mother had read biochemistry and physiology at University College London in the 1930s and was supportive of Johnson’s decision to pursue a scientific career. She went to University College London in 1959 to read Physics and coming from an all-girls school, she was surprised to find herself one of only four girls in a class of 40.
in 1962 she moved to the Royal Institution to do a PhD in biophysics.[citation needed] Her graduate supervisor was David Chilton Phillips, whose team was working on the crystal structure of lysozyme.[citation needed] Her first task was to determine the structure of a sugar molecule, N-Acetylglucosamine, using x-ray diffraction, which she solved within a year. She then moved onto the study of the substrate binding to the protein lysozyme and was part of the team, that discovered the structure of the enzyme lysozyme; this was the third protein structure ever solved by x-ray crystallography, and the first enzyme. She was awarded her PhD in 1965.[1]
She also met Dr. Abdus Salam in 1962 at a antinuclear proliferation meeting in London in 1962, Salam had met Louise Johnson, then a physics undergraduate at University College London (UCL), who was helping with the meeting’s administration. It was what the French call un coup de foudre, an emotional lightning strike, such as Salam had not experienced since seeing the inaccessible Urmilla at Government College, Lahore, some twenty years before. Louise was only 20 years old, and Salam was 36. It should be noted that Ahmadiyya literature never mentions his second wife (girlfriend) and those circumstances (see the Al-Nahl of 1997, which has 200+ pages of data on Dr. Salam, however, they barely mention his second wife and those 2 amazing kids, see page 200, it is nevertheless from a Pakistani newspaper). Dr. Dame Louise Napier Johnson was never his wife, instead a life-long girlfriend.
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She completed her PhD in 1966, after her PhD, she moved to the laboratory of Frederic M. Richards at Yale University for postdoctoral research in 1966. At Yale she worked as part of a team with Frederic M. Richards and Hal Wyckoff on the crystal structure of another enzyme, ribonuclease, which was solved shortly after she left: the fourth protein structure solved.[7]
After her post-doctoral year at Yale, she returned to the UK in 1967 and took up the post of Departmental Demonstrator in the Department of Zoology, University of Oxford. The Professor of Zoology, J.W.R. Pringle, saw zoology as extending from animal studies to molecular studies, and had been partly responsible for bringing David Phillips to Oxford as Professor of Molecular Biophysics. Johnson was able to combine teaching with independent research and continued her work on lysozyme and new crystal studies on other enzymes.
By 1968, this love affair was in full swing, and secretly. However, Dr. Abdus Salam was still married to Amtul Hafeez (she died in 2007, his first-cousin), she was the sister of Col. G.M. Iqbal. Allegedly, Salam and Louise Johnson were married in a Qadiani wedding in London in 1968. An unlikely witness was Paul Mathews, Salam’s long-time research partner and professor at Imperial (See Fraser, “Cosmic Anger”, page 230-231).
______________________________________________________________________________________________
1973 https://en.wikipedia.org/wiki/Louise_Johnson
In 1973 she was appointed University Lecturer, a post which was associated with Somerville College, Oxford. She became an Additional Fellow of the college and the Janet Vaughan Lecturer. She was now able to expand her team of graduate students and post-doctoral researchers. ______________________________________________________________________________________________
1974 https://www.theguardian.com/science/2012/oct/10/louise-johnson
Figure 3. Zoology department, University of Oxford, 1976. Front row: Louise Johnson (third from left), D. C. Phillips (centre), John Pringle (left of D. C. Phillips). Second row: K. Wilson (seventh from left), Irene Weber (sixth from right). ______________________________________________________________________________________________
1978
The phosphorylase work developed and by 1978 the team had discovered its structure and were able to work on its biological control properties. Glycogen phosphorylase is found in muscle and is responsible for mobilising the energy store of glycogen to provide fuel to sustain muscle contraction. In resting muscle the enzyme is switched off to prevent wasteful degradation of the fuel but in response to nervous or hormonal signals the enzyme is switched on almost simultaneously to generate the energy supply. Her research was directed towards understanding the molecular basis of the biological properties of control and catalytic mechanism. Her team used the bright x-ray source generated at the Synchrotron Radiation Source at Daresbury, which provided data that could not be obtained with the home source.
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1982 https://en.wikipedia.org/wiki/Louise_Johnson https://www.theguardian.com/science/2012/oct/10/louise-johnson
She was David Phillips Professor of Molecular Biophysics at the University of Oxford from 1990 to 2007, and later an emeritus professor.[6]
Figure 6. David Phillips and Louise Johnson at the Ciba Foundation in 1991 (with Ben Bax in the background.) (Photograph copyright unknown.)
Figure 7. Chatting with Dorothy Hodgkin shortly after Louise’s election as a Fellow of the Royal Society and to the David Phillips professorship of molecular biophysics, 1990. (Photograph copyright Norman McBeath.)
Figure 8. Louise with Eddy Fischer (left) and Ernst Helmreich (right) on the occasion of a symposium marking her retirement from the David Phillips professorship, September 2007. (Photograph courtesy of Janos Hajdu.) (Online version in colour.)
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2012 https://en.wikipedia.org/wiki/Louise_Johnson
Dame Louise Napier Johnson, DBEFRS (26 September 1940 – 25 September 2012[5]), was a British biochemist and protein crystallographer. She was David Phillips Professor of Molecular Biophysics at the University of Oxford from 1990 to 2007, and later an emeritus professor.[6] She was married to Pakistani nuclear physicist and a Nobel Prize-laureate Abdus Salam.
Johnson attended Wimbledon High School for Girls from 1952 to 1959, where girls were encouraged to study science and to pursue useful careers. Her mother had read biochemistry and physiology at University College London in the 1930s and was supportive of Johnson’s decision to pursue a scientific career. She went to University College London in 1959 to read Physics and coming from an all-girls school, she was surprised to find herself one of only four girls in a class of 40.
She took theoretical physics as her third-year option and graduated with a 2.1 degree. Whilst working at the Atomic Energy Authority, Harwell, on neutron diffraction, during one of her vacations, she met Uli Arndt, an instrument scientist, who worked at the Royal Institution, London. She was impressed by the work taking place there and in 1962 she moved to the Royal Institution to do a PhD in biophysics.[citation needed] Her graduate supervisor was David Chilton Phillips, whose team was working on the crystal structure of lysozyme.[citation needed] Her first task was to determine the structure of a sugar molecule, N-Acetylglucosamine, using x-ray diffraction, which she solved within a year. She then moved onto the study of the substrate binding to the protein lysozyme and was part of the team, that discovered the structure of the enzyme lysozyme; this was the third protein structure ever solved by x-ray crystallography, and the first enzyme. She was awarded her PhD in 1965.[1]
After her PhD, she moved to the laboratory of Frederic M. Richards at Yale University for postdoctoral research in 1966. At Yale she worked as part of a team with Frederic M. Richards and Hal Wyckoff on the crystal structure of another enzyme, ribonuclease, which was solved shortly after she left: the fourth protein structure solved.[7]
After her post-doctoral year at Yale, she returned to the UK in 1967 and took up the post of Departmental Demonstrator in the Department of Zoology, University of Oxford. The Professor of Zoology, J.W.R. Pringle, saw zoology as extending from animal studies to molecular studies, and had been partly responsible for bringing David Phillips to Oxford as Professor of Molecular Biophysics. Johnson was able to combine teaching with independent research and continued her work on lysozyme and new crystal studies on other enzymes. In 1972 she received some crystals of glycogen phosphorylase and this was the beginning of a major chapter in her research career. She began a detailed x-ray crystallographic analysis of the protein, which was eight times larger than lysozyme and much larger than any of the other proteins whose structures had been solved at that time.
In 1973 she was appointed University Lecturer, a post which was associated with Somerville College, Oxford. She became an Additional Fellow of the college and the Janet Vaughan Lecturer. She was now able to expand her team of graduate students and post-doctoral researchers. The phosphorylase work developed and by 1978 the team had discovered its structure and were able to work on its biological control properties. Glycogen phosphorylase is found in muscle and is responsible for mobilising the energy store of glycogen to provide fuel to sustain muscle contraction. In resting muscle the enzyme is switched off to prevent wasteful degradation of the fuel but in response to nervous or hormonal signals the enzyme is switched on almost simultaneously to generate the energy supply. Her research was directed towards understanding the molecular basis of the biological properties of control and catalytic mechanism. Her team used the bright x-ray source generated at the Synchrotron Radiation Source at Daresbury, which provided data that could not be obtained with the home source.[7] She was David Phillips Professor in Molecular Biophysics, University of Oxford, in 1990–2007.
Johnson’s lab at Oxford solved and studied many other protein structures, and she is a depositor on 100 PDB entries including many forms of glycogen phosphorylase[8] and of cell cycle CDK/cyclin complexes[9] As well as carrying out cutting-edge research, she nurtured numerous careers, training a generation of crystallographers in Oxford who themselves now train future leaders across the world.[10] Together with Tom Blundell, she wrote an influential textbook on protein crystallography.[11] She was Director of Life Sciences at Diamond Light Source, 2003–2008, and was a Fellow of Diamond Light Source, 2008–2012. Diamond Light Source is the UK’s national synchrotron facility at Harwell, Oxfordshire.[12]
Louise Napier Johnson was born on 26 September 1940 at South Bank Nursing Home, Worcester, as the second of three daughters of George Edmund Johnson (1904–1992), a wool broker then serving in the Royal Air Force, and his wife, Elizabeth Minna, née King (1914–1992). The family was living at White Cottage, Rushwick, near Worcester, at the time.[17]
Johnson married the Pakistani theoretical physicist Abdus Salam in 1968.[5] He later shared the Nobel Prize for Physics in 1979 for his work on electroweak unification. They had two children: a son born in 1974 and a daughter born in 1982. Johnson’s husband died in 1996. She died on 25 September 2012 in Cambridge, England, aged 71.[18][5][19]
^ Jump up to:abLouise N. Johnson, “Clever Women”, unpublished autobiographical notes, deposited with the papers of L.N. Johnson, at the Bodleian Library, University of Oxford.
^Elspeth F. Garman, “Johnson, Dame Louise Napier (1940–2012)”, Oxford Dictionary of National Biography (Oxford, UK: Oxford University Press, 2016) Retrieved 21 February 2016.
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 died in 1996. Louise is survived by her children.
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