Hugh Esmor Huxley|
25 February 1924
Birkenhead, Cheshire, England
25 July 2013 (aged 89)|
Woods Hole, Massachusetts, US
Christ's College, Cambridge|
Cambridge University (PhD)
William Bate Hardy Prize (1966)|
Louisa Gross Horwitz Prize (1971)
Royal Medal (1977)
Albert Einstein World Award of Science (1987)
Franklin Medal (1990)
Copley Medal (1997)
Massachusetts Institute of Technology|
University College London
MRC Laboratory of Molecular Biology
|Doctoral advisor||John Kendrew|
Hugh Esmor Huxley MBE FRS (25 February 1924 – 25 July 2013) was a British molecular biologist who made important discoveries in the physiology of muscle. He was a graduate in physics from Christ's College, Cambridge. However, his education was interrupted for five years by the Second World War, during which he served in the Royal Air Force. His contribution to development of radar earned him an MBE.
Huxley was the first PhD student of Laboratory of Molecular Biology of the Medical Research Council at Cambridge, where he worked on X-ray diffraction studies on muscle fibres. In the 1950s he was one of the first to use electron microscopy to study biological specimens. During his postdoctoral at Massachusetts Institute of Technology, he, with fellow researcher Jean Hanson, discovered the underlying principle of muscle movement, popularised as the sliding filament theory in 1954. After 15 years of research, he prosposed the "swinging cross-bridge hypothesis" in 1969, which became modern understanding of the molecular basis of muscle contraction, and much of other cellular motility.
Huxley worked at University College London for seven years, and at Laboratory of Molecular Biology for fifteen years, where he was its Deputy Director from 1979. Between 1987 and 1997, he was professor at Brandeis University in Massachusetts, where he spent the rest of his life as emeritus professor.
Huxley studied physics at Christ's College, Cambridge in 1941. During his second year, his education was interrupted by the Second World War, and he joined the Royal Air Force as a radar officer. He worked on the development of radar equipment for during 1943 to 1947, for which he was later honoured a Member of the Order of the British Empire (MBE). His expertise in mechanical and electrical devices became useful throughout his scientific career. After completing his service, he returned to Cambridge for his final year, and he received his BA in physics in 1948. The war had completely diminished his interest in physics, particularly on the horrors of atomic bombings of Hiroshima and Nagasaki. He therefore joined Cambridge University to become the first PhD student in a newly formed Laboratory of Molecular Biology, then a small Medical Research Council MRC unit founded by Max Perutz and John Kendrew, who supervised him. (The LMB was then a small "hut" near the famous Cavendish Laboratory.) He was initially given X-ray analysis of proteins, but he turned to muscle. (The protein study was given to the other student Francis Crick, of the eventual DNA fame.) From there he earned his PhD in 1952 in molecular biology. For his thesis titled Investigations in Biological Structures by X-Ray Methods. The Structure of Muscle, he used low-angle, X-ray scattering of live muscle fibers.
Following his PhD, Huxley continued research on the structure and function of muscle. Since Cambridge did not have electron microscopy, which began to be used for biological studies at the time, he went to Massachusetts Institute of Technology as a postdoctoral fellow on a Commonwealth Fellowship in late summer of 1952. He work in F. O. Schmitt's laboratory where he was joined by Jean Hanson in 1953. Their collaboration proved to be fruitful as they discovered the so-called "sliding filament theory" of muscle contraction. Their publication in the 22 May 1954 issue of Nature became a landmark in muscle physiology. He returned to MRC unit of Cambridge in the late spring of 1954. Using X-ray diffraction he found the molecular interaction in the muscle fibres. The LMB was then equipped with electron microscope, but still had technical issues. Knowing his potential the University College London appointed him to the faculty, and moved there to join Bernard Katz's biophysics department in 1955. For his purpose he was bought a new electron microscope with fund from the Wellcome Trust. His innovative contribution was making a modified version of thin-sectioning microtome, by which he could make histological sections of only 100–150 Å in thickness. Based on his LMB X-ray diffraction images, the new technique immediately helped him to establish the cross-bridge concept (interaction site of the muscle proteins, myosin and actin). As the MRC unit was enlarged he was invited back in 1962, with a research fellowship at King's College for five years and then a more permanent one at Churchill College. He became the joint Head of the Structural Studies Division of the LMB in 1975, and its Deputy Director in 1979. In 1969, on the basis of his work over more than 15 years, he finally formulated the "swinging cross-bridge hypothesis" of muscle contraction, which is the molecular basis of muscle contraction. The concept itself became directly fundamental to other types of cell motility. In 1987 he joined the biology faculty at Brandeis University in Waltham, Massachusetts, where he also served as Director of the Rosenstiel Basic Medical Sciences Research Center, and becoming emeritus from 1997 until his death.
Awards and honours
He was made an MBE in 1948. He was elected member of Fellow of the Royal Society in 1960 (the youngest member at that time). He was awarded the Louisa Gross Horwitz Prize from Columbia University in 1971. He also won one of its Royal Medals in 1977 and its Copley Medal in 1997. The U.S. National Academy of Sciences appointed him as a Foreign Associate in 1978. He also received the William Bate Hardy Prize in 1966, Antonio Feltrinelli Prize, E. B. Wilson Medal of the American Society for Cell Biology in 1983, and the Franklin Medal in 1990. He was conferred the Albert Einstein World Award of Science in 1987 for his contributions to molecular biology, notably his classic work in the field of muscle biology.
Huxley was a Distinguished Supporter of the British Humanist Association. He was among the 43 scientists and philosophers who signed the BHA letter in March 2002 to Prime Minister Tony Blair deploring the teaching of creationism in schools. He also advocated Charles Darwin’s birthday as public holiday, and curricular reforms in elementary science education.
Huxley died of heart attack on 25 July 2013 in his home in Woods Hole, Massachusetts. He is survived by his wife, Frances, his daughter, Olwen, and stepchildren, Bill, Glenway, and Amy Fripp.
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- "Professor Hugh Esmor Huxley MBE FRS | Christs College Cambridge". Christs.cam.ac.uk. 2013-07-25. Retrieved 2013-07-31.
- The Official Site of Louisa Gross Horwitz Prize
- Hugh Huxley, editor "Memories and Consequences: Visiting Scientists at the MRC Laboratory of Molecular Biology, Cambridge", Medical Research Council, 2013, ISBN 978-184831-646-1. This book is collection of 41 essays by some of the many visiting scientists to the MRC LMB in Cambridge, England, during the period 1957-1986.
- John Finch; 'A Nobel Fellow On Every Floor', Medical Research Council 2008, 381 pp, ISBN 978-1-84046-940-0; this book is all about the MRC Laboratory of Molecular Biology, Cambridge.
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- Huxley, H.; Hanson, J. (1954). "Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation". Nature. 173 (4412): 973–976. doi:10.1038/173973a0. PMID 13165698.
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- Huxley, HE (1957). "The double array of filaments in cross-striated muscle". The Journal of Biophysical and Biochemical Cytology. 3 (5): 631–48. doi:10.1083/jcb.3.5.631. PMC . PMID 13475381.
- Huxley, H. E. (1969). "The Mechanism of Muscular Contraction". Science. 164 (3886): 1356–1366. doi:10.1126/science.164.3886.1356. PMID 4181952.
- Huxley, Hugh E. (2004). "Fifty years of muscle and the sliding filament hypothesis". European Journal of Biochemistry. 271 (8): 1403–1415. doi:10.1111/j.1432-1033.2004.04044.x. PMID 15066167.
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