Prof. Jane Clarke

Education:

• 1969 – 1972
  BA 1st Class Honours, Biochemistry, University of York UK
  
  

• 1972 – 1973
  Post-Graduate Certificate of Education, University of Cambridge UK
  
  

• 1987 – 1990
  Part time M.Sc. in Applied Biology, Georgia Institute of Technology, Atlanta, Georgia USA, Thesis title: "Kinetic Study of the Interaction of T7 RNA Polymerase with its Natural Promoters."
  
  

• 1990 – 1993
  PhD, Department of Chemistry and Lucy Cavendish College, University of Cambridge UK, Supervisor, Professor A R Fersht FRS, Thesis title: Disulphide Mutants of Barnase
  
  

Career:

• 1973 – 1986
  Science teacher in secondary schools, including Head of Science post, Northumberland Park School, Tottenham
  
  

• 1994 – 1997
  Postdoctoral Fellow, Centre for Protein Engineering, MRC Centre, Cambridge, Research field – Proteins: Structure, stability and folding, using protein engineering and NMR.
  
  

• 1997 – 2001
  Wellcome Trust Career Development Fellow Folding studies of beta-sandwich proteins
  
  

• 2001 – 2006
  Wellcome Trust Senior Research Fellow Studies of the folding of structurally related proteins – the fold approach
  
  

• since 2001
  University of Cambridge UK
  
  

• 2009
  Reader in Molecular Biophysics
  
  

• 2010
  Fellow of Trinity Hall, Cambridge
  
  

• 2010
  Professor of Molecular Biophysics
  
  

• 2010
  Deputy Head of Department of Chemistry
  
  

• since 2011
  Wellcome Trust Senior Research Fellowship in Basic Biomedical Science Multidisciplinary studies of protein folding, misfolding and assembly.
  
  

• J. Mol. Bio., 2015, 427, 2159-2165

• Nat. Commun., 2015, 6, 7271

• Science, 2014, 346, 6216

• Proc. Natl. Acad. Sci. USA, 2014, 111, 15420–15425

• Proc. Natl. Acad. Sci. USA, 2014, 111, 12055-12060

• J. Am. Chem. Soc., 2014, 136, 5197

• J. Mol. Biol., 2014, 426, 1600

• Nature, 2013, 502(7473), 6323

• J. Mol. Biol., 2014, 426, 21

• J. Phys. Chem. B, 2013, 117, 13346

• Multidisciplinary studies of protein folding, misfolding and assembly

• Fundamental Questions:

  (1) How do proteins fold at the atomistic level and how is misfolding avoided?

  (2) How do changes in sequence, as the result of evolution, or brought about by mutation affect

  the biophysical properties of proteins?

• We study families of proteins using a multidisciplinary approach, to address specific questions:

  (i) What is the relative importance of topology, chain connectivity, secondary structure content and sequence in the folding of small model proteins?

  (ii) How do larger, multidomain proteins fold and, importantly, avoid misfolding?

  (iii) By what mechanisms do intrinsically disordered proteins concomitantly fold and bind to their targets?

• Fellow of Royal Society of Chemistry

• Member of Protein Society

• Member of Biophysical Society

• Member of American Chemical Society

• Member of the International Advisory Board for ChELSI (Chemical Engineering at the Life Sciences Interface), University of Sheffield

• Member of the Wellcome Trust Peer Review College

• Member of Wellcome Trust/NIH Studentship Panel

• Member of Scientific Advisory Board of Astbury Centre Wellcome Trust PhD programme (University of Leeds)

Soft Skills

• Mentoring

• Career Development

• Leadership Training

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