Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Stress relaxation in F-actin solutions by severing.


McCall,  Patrick M
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Arzash, S., McCall, P. M., Feng, J., Gardel, M. L., & MacKintosh, F. C. (2019). Stress relaxation in F-actin solutions by severing. Soft matter, 15(31), 6300-6307. doi:10.1039/c9sm01263j.

Cite as: https://hdl.handle.net/21.11116/0000-0006-7E40-5
Networks of filamentous actin (F-actin) are important for the mechanics of most animal cells. These cytoskeletal networks are highly dynamic, with a variety of actin-associated proteins that control cross-linking, polymerization and force generation in the cytoskeleton. Inspired by recent rheological experiments on reconstituted solutions of dynamic actin filaments, we report a theoretical model that describes stress relaxation behavior of these solutions in the presence of severing proteins. We show that depending on the kinetic rates of assembly, disassembly, and severing, one can observe both length-dependent and length-independent relaxation behavior.