Sheena Radford

Sheena Elizabeth Radford OBE FRS[2] FMedSci[3] is a British biophysicist, and Astbury Professor of Biophysics in the Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology at the University of Leeds.[1][4][5][6]

Sheena Radford

FRS FMedSci
Born
Sheena Elizabeth Radford
Alma mater
Spouse(s)Alan Berry[1]
Awards
Scientific career
Fields
Institutions
ThesisDomains and conformational flexibility in the catalytic mechanism of the 2-oxo acid dehydrogenase complexes (1987)
Websiteastbury.leeds.ac.uk/bmbsgi10

Education

Radford was educated at the University of Birmingham, and the University of Cambridge, where she was awarded a PhD in 1987.[1][7][8]

Research

Radford's research[9] investigates protein folding, protein aggregation and amyloid disease.[10][11][12][13][14][15][16]

Awards and honours

Radford was elected a Fellow of the Royal Society (FRS) in 2014; her nomination reads:

Sheena Radford is internationally distinguished for her seminal contributions to understanding how the dynamical properties of proteins enable them to fold and function biologically, or to misfold and cause degenerative diseases. She has used sophisticated experimental techniques to characterise protein folding pathways in exquisite detail, in particular demonstrating that non-native as well as native-like interactions can play key roles in stabilising partially folded intermediate states. She has built on these findings to define key steps in the aberrant self-assembly of misfolded proteins into amyloid fibrils, particularly in dialysis related amyloidosis, and to relate these molecular processes to pathogenesis.[2]

Radford was elected a Fellow of the Academy of Medical Sciences (FMedSci) in 2010. Her nomination reads:

Sheena Radford is Professor of Structural Molecular Biology at the University of Leeds. Her achievements have involved the innovative application of biophysical techniques to protein folding problems. Her early work in Oxford on hen lysozyme was the foundation for current views that proteins fold on complex multidimensional landscapes, commonly known as folding funnels. She has extended her research to encompass misfolding and disease and has also developed new physical methods to study ultrafast processes. Sheena's work on dialysis-dependent amyloidosis has shown that protein unfolding of beta-2-microglobulin is a key step in fibril formation.[3]

In 1986, Radford was awarded the Colworth Medal from the Biochemical Society. Radford is a member of Faculty of 1000.[17]

Radford was appointed Officer of the Order of the British Empire (OBE) in the 2020 Birthday Honours for services to molecular biology research.[18]

References
  1. Anon (2017). "Radford, Prof. Sheena Elizabeth". Who's Who. ukwhoswho.com (online Oxford University Press ed.). A & C Black, an imprint of Bloomsbury Publishing plc. doi:10.1093/ww/9780199540884.013.U281947. (subscription or UK public library membership required) (subscription required)
  2. Anon (2014). "Professor Sheena Radford FMedSci FRS". London: royalsociety.org. Archived from the original on 2 May 2014.
  3. Anon (2010). "Professor Sheena Radford FRS FMedSci". acmedsci.ac.uk. London: Academy of Medical Sciences. Archived from the original on 6 October 2014.
  4. Sheena Radford's publications indexed by the Scopus bibliographic database. (subscription required)
  5. Folding proteins – from Astbury to Amyloid and Ageing on YouTube
  6. Astbury Centre for Structural Molecular Biology on YouTube
  7. Radford, Sheena Elizabeth (1987). Domains and conformational flexibility in the catalytic mechanism of the 2-oxo acid dehydrogenase complexes. cam.ac.uk (PhD thesis). University of Cambridge. OCLC 53606268. EThOS uk.bl.ethos.236036.
  8. "Prof Sheena Radford | Faculty of Biological Sciences". University of Leeds. Retrieved 10 June 2014.
  9. Sheena Radford ORCID 0000-0002-3079-8039
  10. Booth, D. R.; Sunde, M; Bellotti, V; Robinson, C. V.; Hutchinson, W. L.; Fraser, P. E.; Hawkins, P. N.; Dobson, C. M.; Radford, S. E.; Blake, C. C.; Pepys, M. B. (1997). "Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis". Nature. 385 (6619): 787–93. doi:10.1038/385787a0. PMID 9039909. S2CID 4347837.
  11. Radford, S. E.; Dobson, C. M.; Evans, P. A. (1992). "The folding of hen lysozyme involves partially structured intermediates and multiple pathways". Nature. 358 (6384): 302–7. doi:10.1038/358302a0. PMID 1641003. S2CID 4353275.
  12. Linse, S.; Cabaleiro-Lago, C.; Xue, W. -F.; Lynch, I.; Lindman, S.; Thulin, E.; Radford, S. E.; Dawson, K. A. (2007). "Nucleation of protein fibrillation by nanoparticles". Proceedings of the National Academy of Sciences. 104 (21): 8691–8696. doi:10.1073/pnas.0701250104. PMC 1866183. PMID 17485668.
  13. Brockwell, D. J.; Paci, E.; Zinober, R. C.; Beddard, G. S.; Olmsted, P. D.; Smith, D. A.; Perham, R. N.; Radford, S. E. (2003). "Pulling geometry defines the mechanical resistance of a β-sheet protein". Nature Structural Biology. 10 (9): 731–7. doi:10.1038/nsb968. PMID 12923573. S2CID 7010866.
  14. Dobson, C. M.; Evans, P. A.; Radford, S. E. (1994). "Understanding how proteins fold: The lysozyme story so far". Trends in Biochemical Sciences. 19 (1): 31–7. doi:10.1016/0968-0004(94)90171-6. PMID 8140619.
  15. Miranker, A; Robinson, C. V.; Radford, S. E.; Aplin, R. T.; Dobson, C. M. (1993). "Detection of transient protein folding populations by mass spectrometry". Science. 262 (5135): 896–900. doi:10.1126/science.8235611. PMID 8235611.
  16. Aggeli, A.; Bell, M.; Boden, N.; Keen, J. N.; Knowles, P. F.; McLeish, T. C. B.; Pitkeathly, M.; Radford, S. E. (1997). "Responsive gels formed by the spontaneous self-assembly of peptides into polymeric β-sheet tapes". Nature. 386 (6622): 259–62. doi:10.1038/386259a0. PMID 9069283. S2CID 4343341.
  17. "Sheena Radford: Section Head in Protein Chemistry & Proteomics". f1000.com. Retrieved 10 June 2014.
  18. "No. 63135". The London Gazette (Supplement). 10 October 2020. p. B14.


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