Influence of Hydrodynamic Interactions on Mechanical Unfolding of Proteins

TL;DR

This study investigates how hydrodynamic interactions affect the mechanical unfolding of proteins, revealing that such interactions can both reduce peak forces during stretching and influence unfolding dynamics.

Contribution

It introduces a structure-based model incorporating hydrodynamic interactions, highlighting their significant role in protein unfolding under mechanical stress.

Findings

Hydrodynamic interactions reduce peak unfolding forces at high stretching speeds.

They facilitate unfolding under constant force conditions.

Hydrodynamic effects inhibit stretching caused by fluid flows.

Abstract

We incorporate hydrodynamic interactions in a structure-based model of ubiquitin and demonstrate that the hydrodynamic coupling may reduce the peak force when stretching the protein at constant speed, especially at larger speeds. Hydrodynamic interactions are also shown to facilitate unfolding at constant force and inhibit stretching by fluid flows.