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

• Fletcher, JM, Harniman, RL, Barnes, FRH, Boyle, AL, Collins, A, Mantell, J, Sharp, TH, Antognozzi, M, Booth, PJ, Linden, N, Miles, MJ, Sessions, RB, Verkade, P & Woolfson, DN 2013, ‘Self-assembling cages from coiled-coil peptide modules’. Science, vol 340., pp. 595-599
• Vincent, TL, Green, PJ & Woolfson, DN 2013, ‘LOGICOIL-multi-state prediction of coiled-coil oligomeric state’. Bioinformatics (Oxford, England), vol 29., pp. 69-76

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