SUPERVISOR: Chris OOSTENBRINK

PROJECT ASSIGNED TO: Giovanni POLATO 

Intrinsically Disordered Proteins (IDP) are a group of biomolecules that are difficult to define: their lack of 3D structure is a fundamental problem in crystallographic and cryoEm studies. IDPs are probably best described by broad structural ensembles, rather than single structures. Computational methods and NMR have a crucial role in investigating IDPs

In this project, we propose to use newly developed methodology for atomic-resolution biophysical characterization of two classes of proteins: a) tyrosine hydroxylase (TyrH) as an example of a so called IDR (containing both a structured and an IDP region); b) microtubule associated protein 2c (Map2c) and a fragment of tau protein, representing large IDPs of about 50 kDa. These proteins will be studied in the context of modifications (phosphorylation) and interactions.

Through Molecular Dynamics simulation complemented with advanced experimental techniques (NMR, SAXS) we will gain information about the conformational behavior of IDP.