PhD position in structural proteomics of kinase complexes

The advance of next generation sequencing will allow in the not so far future to resolve genetic maps for all phenotypic variations occurring in the human population. Despite this exciting perspective we still are far away from understanding and modeling phenotypic outcomes from complex genetic alterations, which is key towards the development of personalized approaches in treating human diseases. Proteins operate in the context of protein complexes and large regulatory networks thereof. It is therefore conceivable that disease associated mutations may affect the composition and topology of protein complexes and affect the local protein network they are part of. We will develop and apply quantitative mass spectrometry based technologies to systematically identify changes in disease associated protein modules to better understand the molecular basis of disease mechanism. Specifically we will focus on how disease associated mutations affect complexes containing human protein kinases, the largest protein family affected by cancer associated mutations. Changes in kinase modules will be measured by affinity purification combined with quantitative mass spectrometry (AP-MS) and cross linking mass spectrometry approaches combined with structural modeling will be used to infer changes in the topology of disease associated kinase complexes.

For details, contact Dr.Matthias Gstaiger.