Professor Dek Woolfson

Research summary

The primary basic research interest of the group is the informational aspect of the protein-folding problem; that is, how does the sequence of a protein determine its active, three-dimensional structure or fold?

We tackle this problem using the following multi-disciplinary approach:

1. We use bioinformatics to garner sequence-to-structure relationships from protein sequence and structural databases.
   
   
2. We test the relationships ("rules for protein folding") that we find in two ways: (a) through ab initio protein-structure prediction; and (b) via rational protein design, where we engineer natural protein structures, or design new ones completely from scratch (so-called de novo design).
   
   
3. We then test ...

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Selected publications

• Zaccai, N, Chi, B, Thomson, A, Boyle, AL, Bartlett, G, Bruning, M, Linden, N, Sessions, R, Booth, P, Brady, R & Woolfson, D 2011, ‘A de novo peptide hexamer with a mutable channel’. Nature Chemical Biology, vol 7., pp. 935-941
• Yoshimura, A, Fletcher, J, Yu, Z, Persikov, A, Bartlett, G, Boyle, A, Vincent, T, Woolfson, D & Brodsky, B 2011, ‘Designed Coiled Coils promote folding of a recombinant bacterial collagen’. Journal of Biological Chemistry, vol 286 (20)., pp. 17512 - 17520

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Recent publications

• Sharp, TH, Bruning, M, Mantell, JM, Sessions, RB, Thomson, AR, Zaccai, NR, Brady, RL, Verkade, P & Woolfson, DN 2012, ‘Cryo-transmission electron microscopy structure of a gigadalton peptide fiber of de novo design’. Proceedings of the National Academy of Sciences, vol 109., pp. 13266-13271
• Boyle, AL, Bromley, EHC, Bartlett, GJ, Sessions, RB, Sharp, TH, Williams, C, Curmi, P, Forde, N, Linke, H & Woolfson, DN 2012, ‘Squaring the Circle in Peptide Assembly: From Fibers to Discrete Nanostructures by De Novo Design.’. Journal of the American Chemical Society, vol 134., pp. 15457-15467

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