Departmental Papers (CBE)
Title
Fragility and Mechanosensing in a Thermalized Cytoskeleton Model with Forced Protein Unfolding
Document Type
Journal Article
Date of this Version
November 2007
Abstract
We describe a model of cytoskeletal mechanics based on the force-induced conformational change of protein cross-links in a stressed polymer network. Slow deformation of simulated networks containing cross-links that undergo repeated, serial domain unfolding leads to an unusual state — with many cross-links accumulating near the critical force for further unfolding. This state is robust to thermalization and does not occur in similar protein unbinding based simulations. Moreover, we note that the unusual configuration of near-critical protein cross-links in the fragile state provides a physical mechanism for the chemical transduction of cell-level mechanical strain and extra-cellular matrix stiffness.
Recommended Citation
Hoffman, B. D., Massiera, G., & Crocker, J. C. (2007). Fragility and Mechanosensing in a Thermalized Cytoskeleton Model with Forced Protein Unfolding. Retrieved from https://repository.upenn.edu/cbe_papers/100
Date Posted: 15 January 2008
This document has been peer reviewed.
Comments
Copyright American Physical Society. Reprinted in Physical Review E, Volume 76, Issue 5, Article 051906, November 2007.
Publisher URL: http://link.aps.org/abstract/PRE/v76/e051906