Allostery is a key biological regulatory mechanism which allows the presence of a small molecule, co-factor or protein-binding to regulate the functio

Allostery is a key biological regulatory mechanism which allows the presence of a small molecule, co-factor or protein-binding to regulate the function of a distal enzyme binding site. Allosteric sites are therefore potentially important drug targets as drugging an allosteric site is potentially an alternative to direct drugging of the enzyme active site itself. This can be particularly important for targeting specific proteins of a wider class, such as kinases, where selectivity through direct binding to the active site itself is hard to achieve.
Imperial College researchers have recently developed theoretical methods for the prediction of the presence and location of allosteric sites in proteins. These methods have proven highly successful in identifying and locating known allosteric sites. The aim of this project is to develop methods for rapid, accurate and sensitive experimental screening for the presence and location of predicted, but previously unknown, allosteric sites.
The PhD position is a CASE studentship based at Imperial College for 4 years. The project is a scientific collaboration between a team at Imperial College and a team at AstraZeneca and the successful applicant will also spend time at the AstraZeneca site in Cambridge as necessary for progression of the project.
Applicants should have a good degree in Chemistry or Physics, with an interest in spectroscopy and protein mechanisms.