Influence of Hydrodynamic Interactions on Mechanical Unfolding of Proteins

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.

to be published in Journal of Physics: Condensed Matter

References in corpus (1)

• Stretching of proteins in a uniform flow

Cited by in corpus (4)

• Dodging the crisis of folding proteins with knots
• Proteins in a shear flow
• Hydrodynamic Interactions in Protein Folding
• Effects of confinement and crowding on folding of model proteins