Stretching of proteins in a uniform flow

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...

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Bibliographic Details
Published in:The Journal of chemical physics 2006-10, Vol.125 (16), p.164903-164903-8
Main Authors: Szymczak, P., Cieplak, Marek
Format: Article
Language:English
Subjects:
Models, Biological
Protein Folding
Proteins - chemistry
Proteins - metabolism
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Summary: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.
ISSN:0021-9606
1089-7690
DOI:10.1063/1.2358346