Jane Clarke (scientist)

For other people called Jane Clarke, see Jane Clarke.
Jane Clarke

Jane Clarke in 2015, portrait via the Royal Society
Born Jane Morgan[1]
(1950-09-10) 10 September 1950[1]
London
Fields
Institutions
Alma mater
Thesis Studies of disulphide mutants of barnase (1993)
Doctoral advisor Alan Fersht[2]
Notable students
Notable awards
Spouse Christopher Clarke (m. 1973)[1]
Children one son, one daughter[1]
Website
www-clarke.ch.cam.ac.uk

Jane Clarke, FRS, FRSC, FMedSci (née Morgan; born 10 September 1950) is Professor of Molecular Biophysics, a Wellcome Trust Senior Research Fellow[24] in the Department of Chemistry at the University of Cambridge and a Fellow of Trinity Hall, Cambridge.[25][26]

Education and Career

Clarke was educated at the University of York where she graduated with a first class honours degree in Biochemistry in 1972.[1] She went on to study for a Postgraduate Certificate in Education (PGCE) at the University of Cambridge in 1973.[1] Clarke was a science teacher in several secondary schools, and a Head of Science at Northumberland Park School, Tottenham from 1973 to 1986.

She returned to research, gaining a Master of Science degree in Applied Biology in 1990 from the Georgia Institute of Technology and a PhD in 1993 for investigations of Bacterial Ribonuclease (Barnase) from the University of Cambridge supervised by Alan Fersht.[2][27][28]

Clarke was appointed a Wellcome Trust Senior Research Fellow in 2001, a Professor of Molecular Biophysics in 2009 and a Fellow of Trinity Hall, Cambridge in 2010.[1]

Research

Clarke's research investigates protein folding,[29] in particular:

  1. Studies of Structurally Related Proteins
  2. Multidomain Proteins: Effects of Sequence on Folding and Misfolding
  3. Folding and Assembly: Intrinsically disordered proteins

Clarke's research has been funded by the Wellcome Trust,[24] Medical Research Council (MRC) and the Biotechnology and Biological Sciences Research Council (BBSRC)[30] and has been published in leading peer reviewed scientific journals including Biochemistry,[28] Structure,[31] the Journal of Biological Chemistry, the Biophysical Journal,[18][19][32][33][34][35][36] Nature,[37] Science,[16] PNAS,[38] the Journal of the American Chemical Society,[20][39][40][41] Current Opinion Structural Biology [8][42][43][44][45] and the Journal of Molecular Biology.[46][47]

Awards and honours

In 2010, Clarke was awarded the US Genomics award from the Biophysical Society.[48] Clarke was also elected a Fellow of the Royal Society of Chemistry and a Fellow of the Academy of Medical Sciences (FMedSci) in 2013.[1] Her nomination for the Academy of Medical Sciences reads:

“ Jane Clarke is a distinguished biophysical chemist at the University of Cambridge. She is recognised internationally for her multidisciplinary studies that have advanced the understanding of protein folding and misfolding. She pioneered the application of protein engineering techniques together with single molecule force spectroscopy and simulations to investigate the effect of force on proteins. For this she was awarded the Biophysical Society U.S Genomics Award for Outstanding Investigator in the field of Single Molecule Biology in 2010; at the time, the only non-US and still the only female recipient of this prestigious award.[49] ”

Clarke was elected a Fellow of the Royal Society (FRS) in 2015. Her certificate of election reads:

“ Jane Clarke is distinguished for the rigorous physical chemistry approaches she has adapted and applied to understand protein folding and misfolding. Her fundamental studies revealed the presence of both parallel pathways and frustration in the energy landscape of apparently simple proteins. Most significantly, she has made very important advances in the study of multi-domain systems. From her discovery that aggregation and misfolding are determined by sequence similarity, through to her seminal studies combining force spectroscopy and protein engineering to elucidate mechanical unfolding energy landscapes, she has transformed our understanding of the evolution, folding and energetics of multidomain proteins.[50] ”

Personal life

Clarke married Christopher Clarke in 1973 and has one son and one daughter.[1]

References

  1. 1 2 3 4 5 6 7 8 9 CLARKE, Prof. Jane. Who's Who. 2015 (online Oxford University Press ed.). A & C Black, an imprint of Bloomsbury Publishing plc. (subscription required)
  2. 1 2 "Women at Cambridge: Jane Clarke". University of Cambridge. Archived from the original on 2015-03-24.
  3. ↑ Batey, Sarah (2005). Folding in a multi-domain protein (PhD thesis). University of Cambridge.
  4. ↑ Best, Robert. (2003). High resolution studies of protein folding and dynamics (PhD thesis). University of Cambridge.
  5. ↑ Billings, Kate S. (2007). Studies on core-swapped fibronectin type III domains (PhD thesis). University of Cambridge.
  6. ↑ Cota-Segura, Ernesto (2000). Studies on the folding of the tenth fnIII domain of the human fibronectin (PhD thesis). University of Cambridge.
  7. ↑ Forman, Julia R. (2006). Biophysical investigations of PKD domains : mechanosensation and pathogenesis (PhD thesis). University of Cambridge.
  8. 1 2 Forman, J. R.; Clarke, J (2007). "Mechanical unfolding of proteins: Insights into biology, structure and folding". Current Opinion in Structural Biology. 17 (1): 58–66. doi:10.1016/j.sbi.2007.01.006. PMID 17251000.
  9. ↑ Fowler, Susan B. (2002). Folding studies on an immunoglobulin domain using chemical and mechanical methods (PhD thesis). University of Cambridge.
  10. ↑ Geierhaas, Christian D. (2006). Computational studies of protein folding (PhD thesis). University of Cambridge.
  11. ↑ Hamill, Stephan. J. (2000). Folding and evolution of the immunoglobulin-like superfold (PhD thesis). University of Cambridge.
  12. 1 2 3 "Current and former members of Jane Clarke's laboratory". University of Cambridge. Archived from the original on 2013-02-27.
  13. ↑ Hurley, Mike G. (2007). Analysis and prediction of the protein folding nucleus using computational and experimental techniques (PhD thesis). University of Cambridge.
  14. ↑ Ng, Sean Pin (2006). Biophysical studies of mechanical proteins (PhD thesis). University of Cambridge.
  15. ↑ Perica, Tina (2013). Evolutionary and structural dynamics of protein complexes (PhD thesis). University of Cambridge.
  16. 1 2 Perica, T; Kondo, Y; Tiwari, S. P.; McLaughlin, S. H.; Kemplen, K. R.; Zhang, X; Steward, A; Reuter, N; Clarke, J; Teichmann, S. A. (2014). "Evolution of oligomeric state through allosteric pathways that mimic ligand binding". Science. 346 (6216): 1254346. doi:10.1126/science.1254346. PMC 4337988Freely accessible. PMID 25525255.
  17. ↑ Randles, Lucy Gaynor (2008). Studies of multidomain proteins : effects of force and mutation (PhD thesis). University of Cambridge.
  18. 1 2 Randles, L. G.; Batey, S; Steward, A; Clarke, J (2008). "Distinguishing specific and nonspecific interdomain interactions in multidomain proteins". Biophysical Journal. 94 (2): 622–8. doi:10.1529/biophysj.107.119123. PMC 2157218Freely accessible. PMID 17890397.
  19. 1 2 Randles, L. G.; Rounsevell, R. W.; Clarke, J (2007). "Spectrin domains lose cooperativity in forced unfolding". Biophysical Journal. 92 (2): 571–7. doi:10.1529/biophysj.106.093690. PMC 1751415Freely accessible. PMID 17085494.
  20. 1 2 Rogers, J. M.; Wong, C. T.; Clarke, J (2014). "Coupled folding and binding of the disordered protein PUMA does not require particular residual structure". Journal of the American Chemical Society. 136 (14): 5197–200. doi:10.1021/ja4125065. PMC 4017604Freely accessible. PMID 24654952.
  21. ↑ Rounsevell, Ross William Stanley (2005). Mutational analysis of the mechanical unfolding pathway of TNfn3 (PhD thesis). University of Cambridge. OCLC 890158123.
  22. ↑ Scott, Kathryn Anne (2004). Biophysical studies of multidomain proteins (PhD thesis). University of Cambridge.
  23. ↑ Wensley, Beth Gillian (2009). Investigating the folding of a three-helix bundle protein family (PhD thesis). University of Cambridge.
  24. 1 2 "Senior Research Fellows in Basic Biomedical Science". Wellcome Trust. Archived from the original on 2014-09-18.
  25. ↑ "Professor Jane Clarke FMedSci, Biophysical and structural studies of protein folding". University of Cambridge. Archived from the original on 2014-02-28.
  26. ↑ Jane Clarke's publications indexed by the Scopus bibliographic database, a service provided by Elsevier. (subscription required)
  27. ↑ Clarke, Jane (1993). Studies of disulphide mutants of barnase (PhD thesis). University of Cambridge. OCLC 53666398.
  28. 1 2 Clarke, J; Fersht, A. R. (1993). "Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation". Biochemistry. 32 (16): 4322–9. doi:10.1021/bi00067a022. PMID 8476861.
  29. ↑ "Jane Clarke Laboratory Research Areas". University of Cambridge. Archived from the original on 2013-01-26.
  30. ↑ "UK Government Grants awarded Jane Clarke". Research Councils UK. Archived from the original on 2015-04-13.
  31. ↑ Clarke, J.; Cota, E.; Fowler, S. B.; Hamill, S. J. (1999). "Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway". Structure. 7 (9): 1145–1153. doi:10.1016/S0969-2126(99)80181-6.
  32. ↑ Shammas, S. L.; Rogers, J. M.; Hill, S. A.; Clarke, J (2012). "Slow, reversible, coupled folding and binding of the spectrin tetramerization domain". Biophysical Journal. 103 (10): 2203–14. doi:10.1016/j.bpj.2012.10.012. PMC 3512043Freely accessible. PMID 23200054.
  33. ↑ Geierhaas, C. D.; Best, R. B.; Paci, E; Vendruscolo, M; Clarke, J (2006). "Structural comparison of the two alternative transition states for folding of TI I27". Biophysical Journal. 91 (1): 263–75. doi:10.1529/biophysj.105.077057. PMC 1479071Freely accessible. PMID 16603501.
  34. ↑ Batey, S; Scott, K. A.; Clarke, J (2006). "Complex folding kinetics of a multidomain protein". Biophysical Journal. 90 (6): 2120–30. doi:10.1529/biophysj.105.072710. PMC 1386790Freely accessible. PMID 16387757.
  35. ↑ Best, R. B.; Li, B; Steward, A; Daggett, V; Clarke, J (2001). "Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation". Biophysical Journal. 81 (4): 2344–56. doi:10.1016/S0006-3495(01)75881-X. PMC 1301705Freely accessible. PMID 11566804.
  36. ↑ Rounsevell, R. W.; Steward, A; Clarke, J (2005). "Biophysical investigations of engineered polyproteins: Implications for force data". Biophysical Journal. 88 (3): 2022–9. doi:10.1529/biophysj.104.053744. PMC 1305254Freely accessible. PMID 15613637.
  37. ↑ Wright, C. F.; Teichmann, S. A.; Clarke, J.; Dobson, C. M. (2005). "The importance of sequence diversity in the aggregation and evolution of proteins". Nature. 438 (7069): 878–81. doi:10.1038/nature04195. PMID 16341018.
  38. ↑ Carrion-Vazquez, M; Oberhauser, A. F.; Fowler, S. B.; Marszalek, P. E.; Broedel, S. E.; Clarke, J; Fernandez, J. M. (1999). "Mechanical and chemical unfolding of a single protein: A comparison". Proceedings of the National Academy of Sciences of the United States of America. 96 (7): 3694–9. doi:10.1073/pnas.96.7.3694. PMC 22356Freely accessible. PMID 10097099.
  39. ↑ Borgia, M. B.; Nickson, A. A.; Clarke, J; Hounslow, M. J. (2013). "A mechanistic model for amorphous protein aggregation of immunoglobulin-like domains". Journal of the American Chemical Society. 135 (17): 6456–64. doi:10.1021/ja308852b. PMC 3759167Freely accessible. PMID 23510407.
  40. ↑ Rogers, J. M.; Steward, A; Clarke, J (2013). "Folding and binding of an intrinsically disordered protein: Fast, but not 'diffusion-limited'". Journal of the American Chemical Society. 135 (4): 1415–22. doi:10.1021/ja309527h. PMC 3776562Freely accessible. PMID 23301700.
  41. ↑ Best, R. B.; Clarke, J; Karplus, M (2004). "The origin of protein sidechain order parameter distributions". Journal of the American Chemical Society. 126 (25): 7734–5. doi:10.1021/ja049078w. PMID 15212494.
  42. ↑ Nickson, A. A.; Wensley, B. G.; Clarke, J (2013). "Take home lessons from studies of related proteins". Current Opinion in Structural Biology. 23 (1): 66–74. doi:10.1016/j.sbi.2012.11.009. PMC 3578095Freely accessible. PMID 23265640.
  43. ↑ Clarke, J; Schief, W (2012). "Learning from Nature to design new biomolecules". Current Opinion in Structural Biology. 22 (4): 395–6. doi:10.1016/j.sbi.2012.07.001. PMID 22858055.
  44. ↑ Clarke, J; Regan, L (2010). "Protein engineering and design: From first principles to new technologies". Current Opinion in Structural Biology. 20 (4): 480–1. doi:10.1016/j.sbi.2010.07.001. PMID 20708403.
  45. ↑ Clarke, J; Itzhaki, L. S. (1998). "Hydrogen exchange and protein folding". Current Opinion in Structural Biology. 8 (1): 112–8. doi:10.1016/s0959-440x(98)80018-3. PMID 9519304.
  46. ↑ Batey, S; Clarke, J (2008). "The folding pathway of a single domain in a multidomain protein is not affected by its neighbouring domain". Journal of Molecular Biology. 378 (2): 297–301. doi:10.1016/j.jmb.2008.02.032. PMC 2828540Freely accessible. PMID 18371978.
  47. ↑ Batey, S; Randles, L. G.; Steward, A; Clarke, J (2005). "Cooperative folding in a multi-domain protein". Journal of Molecular Biology. 349 (5): 1045–59. doi:10.1016/j.jmb.2005.04.028. PMID 15913648.
  48. ↑ "US Genomics Award". Biophysical Society. Archived from the original on 2015-04-08.
  49. ↑ "Professor Jane Clarke FMedSci". London: The Academy of Medical Sciences. Archived from the original on 2015-04-08.
  50. ↑ "Professor Jane Clarke FMedSci FRS". London: Royal Society. Archived from the original on 2015-05-04.
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