Chris Dobson

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Chris Dobson
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Dobson in 2014
Christopher Martin Dobson

(1949-10-08)8 October 1949
Died8 September 2019(2019-09-08) (aged 69)
Sutton, London, England
Alma mater
Scientific career
Thesis The conformation of lysozyme in solution  (1975)

Sir Christopher Martin Dobson, FRS , FMedSci (8 October 1949 – 8 September 2019) was a British chemist, who was the John Humphrey Plummer Professor of Chemical and Structural Biology in the Department of Chemistry at the University of Cambridge, and Master of St John's College, Cambridge. [1] [2]

Fellow of the Royal Society Elected Fellow of the Royal Society, including Honorary, Foreign and Royal Fellows

Fellowship of the Royal Society is an award granted to individuals that the Royal Society of London judges to have made a 'substantial contribution to the improvement of natural knowledge, including mathematics, engineering science, and medical science'.

Fellow of the Academy of Medical Sciences award for fellows who are recognised for the excellence of their science, their contribution to medicine and society and the range of their achievements

Fellowship of the Academy of Medical Sciences (FMedSci) is an award for medical scientists who are judged by the Academy of Medical Sciences for the "excellence of their science, their contribution to medicine and society and the range of their achievements".

Chemistry scientific discipline

Chemistry is the scientific discipline involved with elements and compounds composed of atoms, molecules and ions: their composition, structure, properties, behavior and the changes they undergo during a reaction with other substances.


Early life and education

Dobson was born on 8 October 1949 in Germany, where his father, Arthur Dobson was commissioned as an officer. [3] [4] Both Arthur Dobson and Christopher Dobson's mother, Mabel Dobson (née Pollard), were originally from Bradford in Yorkshire and had left school at age 14. [4] Dobson had two older siblings, Graham and Gillian. [4] Due to his father's postings, Dobson also lived in Lagos, Nigeria. [4]

Germany Federal parliamentary republic in central-western Europe

Germany, officially the Federal Republic of Germany, is a country in Central and Western Europe, lying between the Baltic and North Seas to the north and the Alps, Lake Constance and the High Rhine to the south. It borders Denmark to the north, Poland and the Czech Republic to the east, Austria and Switzerland to the south, France to the southwest, and Luxembourg, Belgium and the Netherlands to the west.

Bradford City and metropolitan borough in England

Bradford is a city in West Yorkshire, England, in the foothills of the Pennines, 8.6 miles (14 km) west of Leeds, and 16 miles (26 km) north-west of Wakefield. Bradford became a municipal borough in 1847, and received its charter as a city in 1897. Following local government reform in 1974, city status was bestowed upon the City of Bradford metropolitan borough.

Yorkshire Historic county of Northern England

Yorkshire, formally known as the County of York, is a historic county of Northern England and the largest in the United Kingdom. Due to its great size in comparison to other English counties, functions have been undertaken over time by its subdivisions, which have also been subject to periodic reform. Throughout these changes, Yorkshire has continued to be recognised as a geographical territory and cultural region. The name is familiar and well understood across the United Kingdom and is in common use in the media and the military, and also features in the titles of current areas of civil administration such as North Yorkshire, South Yorkshire, West Yorkshire and East Riding of Yorkshire.

Christopher Dobson was educated at Hereford Cathedral Junior School, and then Abingdon School from 1960 until 1967. [4] [5] He completed a Bachelor of Arts and D.Phil [6] at the University of Oxford (Keble and Merton Colleges, respectively). [4]

Hereford Cathedral Junior School school in Herefordshire, UK

Hereford Cathedral Junior School is an independent, co-educational day school for children aged from three to eleven years. The Junior School is part of the Hereford Cathedral Foundation and has been under the aegis of the governors of Hereford Cathedral School since 1987.

Abingdon School independent school for boys in Abingdon, Oxfordshire, England

Abingdon School is a day and boarding independent school for boys in Abingdon, Oxfordshire, England. The twentieth oldest independent British school, it celebrated its 750th anniversary in 2006.

A Bachelor of Arts is a bachelor's degree awarded for an undergraduate course or program in either the liberal arts, sciences, or both. Bachelor of Arts programs generally take three to four years depending on the country, institution, and specific specializations, majors, or minors. The word baccalaureus should not be confused with baccalaureatus, which refers to the one- to two-year postgraduate Bachelor of Arts with Honors degree in some countries.


Dobson's research largely focused on protein folding and protein misfolding, and its association with medical disorders particularly Alzheimer's and Parkinson's diseases. By applying chemical and biophysical techniques, Dobson investigated links between protein structure, function, and disease.

Protein folding the process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure

Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner. It is the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure from random coil. Each protein exists as an unfolded polypeptide or random coil when translated from a sequence of mRNA to a linear chain of amino acids. This polypeptide lacks any stable (long-lasting) three-dimensional structure. As the polypeptide chain is being synthesized by a ribosome, the linear chain begins to fold into its three-dimensional structure. Folding begins to occur even during translation of the polypeptide chain. Amino acids interact with each other to produce a well-defined three-dimensional structure, the folded protein, known as the native state. The resulting three-dimensional structure is determined by the amino acid sequence or primary structure.

Alzheimers disease Progressive, neurodegenerative disease characterized by memory loss

Alzheimer's disease (AD), also referred to simply as Alzheimer's, is a chronic neurodegenerative disease that usually starts slowly and gradually worsens over time. It is the cause of 60–70% of cases of dementia. The most common early symptom is difficulty in remembering recent events. As the disease advances, symptoms can include problems with language, disorientation, mood swings, loss of motivation, not managing self-care, and behavioural issues. As a person's condition declines, they often withdraw from family and society. Gradually, bodily functions are lost, ultimately leading to death. Although the speed of progression can vary, the typical life expectancy following diagnosis is three to nine years.

Parkinsons disease Long-term degenerative neurological disorder that mainly causes problems with movement and balance

Parkinson's disease (PD) is a long-term degenerative disorder of the central nervous system that mainly affects the motor system. As the disease worsens, non-motor symptoms become more common. The symptoms usually emerge slowly. Early in the disease, the most obvious symptoms are shaking, rigidity, slowness of movement, and difficulty with walking. Thinking and behavioral problems may also occur. Dementia becomes common in the advanced stages of the disease. Depression and anxiety are also common, occurring in more than a third of people with PD. Other symptoms include sensory, sleep, and emotional problems. The main motor symptoms are collectively called "parkinsonism", or a "parkinsonian syndrome".

He is well-known for his serendipitous discovery that ordinary proteins can misfold and aggregate to form amyloid structures. [4]

Amyloid insoluble protein aggregate

Amyloids are aggregates of proteins that become folded into a shape that allows many copies of that protein to stick together, forming fibrils. In the human body, amyloids have been linked to the development of various diseases. Pathogenic amyloids form when previously healthy proteins lose their normal physiological functions and form fibrous deposits in plaques around cells which can disrupt the healthy function of tissues and organs.

“A postdoc who left his sample of an unfolded protein in an NMR [nuclear magnetic resonance] spectrometer over a long weekend discovered, on his return, that it had turned into a gel. We were curious about this phenomenon and found that the NMR tube was full of amyloid fibrils that we then thought were associated only with diseases.”

Dobson authored and co-authored over 800 papers and review articles, [7] including 38 in Nature , Science and Cell, which have been cited over 100,000 times. [8] . His H-index is 135. [8]

<i>Nature</i> (journal) British multidisciplinary scientific journal

Nature is a British multidisciplinary scientific journal, first published on 4 November 1869. It is one of the most recognizable scientific journals in the world, and was ranked the world's most cited scientific journal by the Science Edition of the 2010 Journal Citation Reports and is ascribed an impact factor of 43.070, making it one of the world's top academic journals. It is one of the few remaining academic journals that publishes original research across a wide range of scientific fields.

Cell is a peer-reviewed scientific journal publishing research papers across a broad range of disciplines within the life sciences. Areas covered include molecular biology, cell biology, systems biology, stem cells, developmental biology, genetics and genomics, proteomics, cancer research, immunology, neuroscience, structural biology, microbiology, virology, physiology, biophysics, and computational biology. The journal was established in 1974 by Benjamin Lewin and is published twice monthly by Cell Press, an imprint of Elsevier.


Dobson held Research Fellowships at Merton College and then Linacre College before working at Harvard University. He returned to Oxford in 1980 as a Fellow of Lady Margaret Hall, Oxford and as a University Lecturer in Chemistry, later receiving promotions to Reader, then Professor of Chemistry in 1996. [3] [4]

Dobson moved to the University of Cambridge in 2001 as the John Humphrey Plummer Professor of Chemical and Structural Biology. In 2007, he became the Master of St John's College, Cambridge, a post which he held until his death in September 2019. [4] [9]

In 2012, Dobson founded the Cambridge Centre for Misfolding Diseases [4] , which is currently based in the Chemistry of Health building at the Department of Chemistry at the University of Cambridge. [9] [10]

In 2016, Chris Dobson co-founded Wren Therapeutics, a biotechnology start-up company whose mission is to find new therapeutics for Alzheimer's disease. [11] [12]

Awards and honours

Professor Dobson was knighted in the 2018 Queen’s Birthday Honours for his contributions to science and higher education. [7] [11] [13] In 2009, Dobson was awarded the Royal Medal by the Royal Society "for his outstanding contributions to the understanding of the mechanisms of protein folding and mis-folding, and the implications for disease", and in 2014 he received both the Heineken Prize for Biochemistry and Biophysics and the Feltrinelli International Prize for Medicine. Dobson was elected a Fellow of the Royal Society (FRS) in 1996. His nomination reads:

Dobson is distinguished for his studies, principally using NMR methods, of the structures and dynamics of proteins in solution. Such studies include those on lysozyme, with which he demonstrated many methodological advances, interleukin-4, with which he established for the first time the topology of the important family of haemopoietic helical cytokines, and urokinase-type plasminogen activator, with which he elucidated the dynamic characteristics of multidomain fibrinolytic proteins, Dobson is a pioneer in the application of NMR methods to the problem of protein folding, which is now the major theme of his work. His studies on lysozyme are resulting in one of the most detailed descriptions of a folding pathway for a protein. Dobson has explored the properties and reactions of molecules in solids by means of NMR spectroscopy, including proteins, organometallic compounds, inorganic paramagnets and the silicaceous components of hydraulic materials. Notable here are analyses of the nature and origin of dynamic properties in molecular solids, and their relationship to structure and reactivity. [14]

Dobson's other accolades include:


Dobson mentored many notable PhD students and post-doctoral researchers, many of whom became renowned experts in the their own field. These include:

Personal life

Dobson met his wife, Dr Mary Dobson (née Schove) at Merton College at the University of Oxford. [4] They had two sons, Richard and William. [7] [9]

He died on 8 September 2019, from cancer, at Royal Marsden Hospital in Sutton, near Surrey. [7]

See also

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  1. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 "Chris Dobson - CV" . Retrieved 11 September 2019.
  2. List of publications from Microsoft Academic
  3. 1 2 "DOBSON, Prof. Christopher Martin". Who's Who . 2014 (online Oxford University Press ed.). A & C Black, an imprint of Bloomsbury Publishing plc.(subscription or UK public library membership required)(subscription required)
  4. 1 2 3 4 5 6 7 8 9 10 11 "Professor Sir Chris Dobson obituary". The Times. 12 September 2019. ISSN   0140-0460 . Retrieved 13 September 2019.
  5. "Chemistry Prizes" (PDF). The Abingdonian.
  6. Dobson, Christopher Martin (2014). The conformation of lysozyme in solution (DPhil thesis). University of Oxford.
  7. 1 2 3 4 "Professor Sir Christopher Dobson, master of St John's College, Cambridge, dies at 69". Cambridge Independent. 9 September 2019. Retrieved 9 September 2019.
  8. 1 2 Chris Dobson's publications indexed by the Scopus bibliographic database. (subscription required)
  9. 1 2 3 "Tributes paid to Master of St John's College who has died age 69". St John's College Cambridge. Retrieved 9 September 2019.
  10. "New research facility for neurodegenerative disorders opened in Cambridge". University of Cambridge. 21 September 2018. Retrieved 9 September 2019.
  11. 1 2 "Knighthood for Prof Christopher Dobson, master of St John's College, in recognition of ground-breaking Alzheimer's research". Cambridge Independent. 8 June 2018. Retrieved 9 September 2019.
  12. "Cambridge spinout grabs $23M round to launch a new campaign to tackle protein misfolding". Endpoints News. Retrieved 9 September 2019.
  13. "Knighthood for eminent scientist Sir Christopher Dobson". Lady Margaret Hall. Retrieved 9 September 2019.
  14. "EC/1996/06: Dobson, Christopher Martin". London: The Royal Society. Archived from the original on 30 September 2014. Retrieved 30 September 2014.
  15. "Bijvoet Medal". Bijvoet Center for Biomolecular Research. Retrieved 12 September 2017.
  16. "Master receives Honorary Degree from King's College London | StJohns".
  17. "Fellows & Scholars : Trinity College Dublin, the University of Dublin, Ireland".
  18. "2013 NAS Members and Foreign Associates Elected".
  19. "Christopher M. Dobson — KNAW".
  20. "Feltrinelli International Prize awarded to Chris Dobson | Department of Chemistry".
  21. "Election of New Members at the 2018 Spring Meeting | American Philosophical Society".
  22. "Paying tribute to Chris Dobson". Retrieved 16 September 2019.
Academic offices
Preceded by
Richard Perham
Master of St John's College, Cambridge
Succeeded by