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

变质是一种关键的生物调节机制，它允许小分子、辅助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点，因为对变构位点进行药物治疗可能是直接对酶活性位点本身进行药物治疗的替代方法。这对于靶向更广泛类别的特定蛋白质尤其重要，例如激酶，其中通过直接结合活性位点本身很难实现选择性。帝国理工学院的研究人员最近开发了理论方法来预测蛋白质中变构位点的存在和位置。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、准确和敏感的实验筛选方法，用于预测但以前未知的变构位点的存在和位置。该博士职位为CASE奖学金，在帝国理工学院学习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现场进行必要的项目进展。申请者应具有化学或物理专业的良好学位，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.