SUPERVISOR: Chris OOSTENBRINK

PROJECT ASSIGNED TO: Johannes STÖCKELMAIER 

The project aims to improve understanding and quality of simulation of intrinsically disordered proteins (IDPs). In the last several years many examples of proteins were discovered that do not feature a fully stable conformation but are intrinsically disordered, challenging the long-established theory of structure-function relationship in biochemistry. To get more insight into the function of IDPs and proteins containing disordered regions (IDRs), proper characterization of this class of proteins is necessary. Because of the physical properties of IDPs, it is expected that a sufficient understanding of IDPs is only possible with support of advanced computational methods.

The computational methods developed during this project will be tested against tyrosine hydroxylase (TyrH), microtubule associated protein 2c (Map2c) and its homologous tau protein. The methods will be designed to be applied to more proteins outside of the examples described in this project and can support pharmaceutical research in the future.