Dynamics, kinetics and assembly of model intrinsically disordered proteins from a polymer physics perspective – IDPXN

Supramolecular assemblies of intrinsically disordered proteins (IDPs), i.e. of proteins lacking a stable 3D-structure, are important in cellular signaling and spatial organization and can be involved in pathologies. Here, we wish to explore the dynamics and kinetics of such assembly processes of IDPs to understand the fundamental mechanisms behind IDP-related diseases. Using the model systems a, ß, and kappa-casein (all disordered), ß-lactoglobulin and apo-myoglobin (both ordered), we intend to establish their respective phase diagrams in solution, to determine the parameter space leading to the formation of supramolecular IDP assemblies, and to quantify the influence of protein disorder on these assembly pathways, as well as to compare chemically and thermally denatured proteins. This project systematically combines advanced x-ray and neutron scattering methods, notably accessing dynamics on the molecular level during kinetics, as well as theory.