Influence of hydrodynamic interactions on mechanical unfolding of proteins

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 co...

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Bibliographic Details
Published in:Journal of physics. Condensed matter 2007-07, Vol.19 (28), p.285224-285224 (12)
Main Authors: Szymczak, P, Cieplak, Marek
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Miscellaneous
Proteins
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Summary: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.
ISSN:0953-8984
1361-648X
DOI:10.1088/0953-8984/19/28/285224