The primary basic research interests of the group are: (A) 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?  And (B), how can we use this information to design completely new proteins from scratch?  In addition, we design proteins for applications in synthetic biology and medicine.

We tackle these problems 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 our engineered and design proteins experimentally using biophysical methods. The peptides and proteins are made either by peptide synthesis, or via recombinant DNA methods and the expression of synthetic genes. The products and then characterised using methods including: solution-phase biophysics (CD, FT-IR and fluorescence spectroscopy, AUC and ITC); high-resolution structural biology (NMR spectroscopy and X-ray crystallography); and microscopy (EM, AFM and light microscopy).
   
   
4. Finally, we explore potential applications of some the engineered and designed proteins in the burgeoning fields of bionanotechnology and synthetic biology.

Professor Woolfson is a supervisor in the EPSRC Centre for Doctoral Training in Chemical Synthesis