Stretching of proteins in a uniform flow

Abstract

Stretching of a protein by a fluid flow is compared to that in a force-clamp apparatus. The comparison is made within a simple topology-based dynamical model of a protein in which the effects of the flow are implemented using Langevin dynamics. We demonstrate that unfolding induced by a uniform flow shows a richer behavior than that in the force clamp. The dynamics of unfolding is found to depend strongly on the selection of the amino acid, usually one of the termini, which is anchored. These features offer potentially wider diagnostic tools to investigate structure of proteins compared to experiments based on the atomic force microscopy.

J. Chem. Phys. (in press)

References in corpus (5)

• Boundary conditions at a fluid - solid interface
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• Sequencing of folding events in Go-like proteins
• Nanoscale fluid flows in the vicinity of patterned surfaces
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