An interdisciplinary approach to model the interaction and binding of flexible proteins: Applications to SARS-CoV-2 accessory proteins'

The dynamics of proteins play critical roles for functions and interactions. Traditional
structural biology provides limited insights on highly flexible, yet functional, regions since
these are absent in most crystal- and cryo-EM structures. NMR spectroscopy, molecular
dynamics simulations and molecular biology will be combined in this project to characterise
how flexible proteins interact with their binding partners. Focus will be on the blood
glycoprotein von Willebrand factor and its binding partners, for example Factor VIII, where
the disordered a3 domain is imperative for high-affinity binding. This project is highly
interdisciplinary, involving substantial elements of computational modelling, NMR and wet-lab
work.