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

变构是一种关键的生物调节机制，其允许小分子、辅因子或蛋白质结合的存在来调节远端酶结合位点的功能。因此，变构位点是潜在的重要药物靶标，因为给变构位点用药是直接给酶活性位点本身用药的潜在替代方案。这对于靶向更广泛类别的特定蛋白质（例如激酶）特别重要，其中通过直接结合到活性位点本身的选择性很难实现。帝国理工学院的研究人员最近开发了预测蛋白质中变构位点的存在和位置的理论方法。这些方法已被证明在识别和定位已知的变构位点方面非常成功。该项目的目的是开发快速，准确和灵敏的实验筛选预测的，但以前未知的，变构位点的存在和位置的方法。博士学位是在帝国理工学院的CASE学生4年。该项目是帝国理工学院的一个团队和阿斯利康的一个团队之间的科学合作，成功的申请人还将在剑桥的阿斯利康工厂工作一段时间，以促进项目的进展。申请人应具有化学或物理学的良好学位，对光谱学和蛋白质机制感兴趣。

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.