Proteins can interact with small molecules at multiple sites on their surfaces; the primary, orthosteric site, where the ligand is directly linked to the function of the protein, and allosteric sites in which the binding causes a functional effect at a distant site. My research looks at these allosteric sites, understanding how local conformational changes are associated with allosteric action. My research will utilise crystallographic fragment screening, where small fragment compounds are soaked with crystals, to determine features which are conserved over many datasets, and which vary when the fragments are bound. Analysis of multiple datasets of the same protein should allow for confidence in detection of features that are present with and without ligands bound at the allosteric site.</p>