Department of Biochemistry University of Oxford Department of Biochemistry
University of Oxford
South Parks Road
Oxford OX1 3QU

Tel: +44 (0)1865 613200
Fax: +44 (0)1865 613201
Image showing the global movement of lipids in a model planar membrane
Matthieu Chavent, Sansom lab
Anaphase bridges in fission yeast cells
Whitby lab
Lactose permease represented using bending cylinders in Bendix software
Caroline Dahl, Sansom lab
Epithelial cells in C. elegans showing a seam cell that failed to undergo cytokinesis
Serena Ding, Woollard lab
Collage of Drosophila third instar larva optic lobe
Lu Yang, Davis lab
First year Biochemistry students at a practical class
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Sarah Shammas
Role of protein disorder within transcriptional regulation

Co-workers: TBA

A significant proportion of eukaryotic proteins contain long disordered regions, which have no single stable structure and instead populate a myriad of highly heterogenous conformations that interchange very rapidly. These proteins are still functional within the cell. The particular over-representation of protein disorder within transcription factors suggests an important biological role for disorder within transcription factors. How functionally important is protein disorder for these critical regulatory proteins, why, and through what mechanism(s)?

Shammas lab uses biophysical assays, and in particular kinetic studies, to address the mechanism of interactions between transcription factors and their binding partners e.g. transcriptional coactivators and DNA. By combining the results of these studies with our findings from molecular dynamics simulations, structural biology (NMR and ESR), and in vivo imaging we examine the role of protein disorder within transcriptional regulation.


  1. Shammas, S.L.*, Crabtree, M.D., Dahal, L., Wicky, B.I.M, Clarke, J. (2016) "Insights into coupled folding and binding mechanisms from kinetics studies". Jour Biol Chem 291, 6689-6695
  2. Milles, S., Mercadante, D., Aramburu, I., Jensen, M.R., Banterle, N., Koehler, C., Clarke, J., Shammas, S.L., Blackledge, M., Grater, F., Lemke, E. (2015) "Plasticity of an ultrafast interaction between nucleoporin and transport receptors". Cell 163, 734-745.
  3. Shammas, S.L.*, Travis, A.J., Clarke J., (2014). "Allostery within a transcriptional coactivator is predominantly mediated through dissociation rates." Proc Natl Acad Sci USA 111, 12055-12060.
  4. Shammas, S.L. , Travis, A.J., Clarke, J. (2013). "Remarkably Fast Coupled Folding and Binding of the Intrinsically Disordered Transactivation Domain of cMyb to CBP KIX." J Phys Chem B117 (42): 13346-13356
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