Sarah Perrett
Institute of Biophysics
Chinese Academy of Sciences
China
Biography
1992    BA in Chemistry, University of Cambridge, UK 1997    PhD in Protein Chemistry, University of Cambridge 1996-1997  Post-Doctoral Research Associate, University of Cambridge 1997-2000  College Research Fellow, University of Cambridge 1999-2000  Chinese language study, National University of Singapore 2000-2003  1851 & Royal Society Research Fellow, CAS Institute of Biophysics, Beijing 2003-present Principal Investigator, CAS Institute of Biophysics 1992    BA in Chemistry, University of Cambridge, UK 1997    PhD in Protein Chemistry, University of Cambridge 1996-1997  Post-Doctoral Research Associate, University of Cambridge 1997-2000  College Research Fellow, University of Cambridge 1999-2000  Chinese language study, National University of Singapore 2000-2003  1851 & Royal Society Research Fellow, CAS Institute of Biophysics, Beijing 2003-present Principal Investigator, CAS Institute of Biophysics
Research Interest
1. Folding and Assembly of Functional Amyloids We are studying the detailed mechanism of fibril assembly for functional amyloids, such as the yeast prion protein Ure2 and the bacterial Chaplin proteins, in order to understand how biological systems regulate protein folding and misfolding. 2. Protein Folding, Post-Translational Modification & Quality Control We are studying the detailed mechanisms by which molecular chaperones control protein folding and misfolding. In particular, we are examining the role of post-translational modification of the molecular chaperone Hsp70 in regulating its structure and function. 3. Biological Properties of Nanomaterials We are studying how the unique properties of amyloid can be exploited in the design of novel nanomaterials. Conversely, we are examining how nanomaterials that are widely used in medical applications interact with amyloidogenic proteins and affect their folding and misfolding.
Publications
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Zhang, H., Yang, J., Si, W., Gong, W., Chen, C.* & Perrett, S.* (2016). Glutathionylation of the bacterial Hsp70 chaperone DnaK provides a link between oxidative stress and the heat shock response. J. Biol. Chem. 291, 6967-6981.