The Towse group uses experimental and computational approaches to arrive at answers regarding protein and peptide structural changes, dynamics and interactions. Our lab specialises in solid-phases peptide synthesis, biophysical characterisation and molecular dynamics simulations. A range of computational tools, such as MODELLER, Autodock, GROMACS and AMBER, are used to perform de novo and templated peptide design, docking, and simulations of protein unfolding, self-assembly, biomolecule interactions and aggregation.
Post-translational Modifications and Amyloidogenesis
The main focus of our research group is in determining conformational consequences of post-translational modifications in proteins and peptides. Our main area of study is determining if some post-translational modifications result in aggregation-prone conformations that could play a role in amyloid diseases. Our group is currently investigating amino acid isomerisation, SUMOylation, phosphorylation and ubiquitination.
Non-natural Amino Acid Propensities
Non-natural amino acids are an interesting solution to peptide drug design. Incorporating non-natural amino acids into peptides and proteins can allow control of active site conformations, alter protein folding behaviour and increase their bio-availability by reducing the susceptibility to proteolytic degradation. We are interested in studying the conformational propensities of non-natural amino acids in order to identify ways in which design of controlled conformations can be managed. In collaboration with the Martin group a recent project is examining the conformational properties of novel non-natural amino acids.