How hydrodynamic interactions affect protein unfolding

What is it about?

Significant effort is being put into accurate treatment of water molecules in atom-scale Molecular Dynamics (MD) simulations of biomolecules. At the same time, in coarse-grained Go-like protein models even mechanistic effects of water are usually limited to random kicks. In this paper we study how inclusion of long-range hydrodynamic interactions (e.g. movement of one protein domain causing movement of water affecting other protein domains) alter dynamic behavior of proteins.

Featured Image

Why is it important?

Our finding show that accounting for hydrodynamic interaction drastically changes dynamic properties of proteins, by accelerating mechanical unfolding and increasing coupling between adjacent domains.