Journal
NEW JOURNAL OF PHYSICS
Volume 14, Issue -, Pages -Publisher
IOP PUBLISHING LTD
DOI: 10.1088/1367-2630/14/3/033037
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Funding
- NSF DMR-MRSEC [0820054]
- Direct For Mathematical & Physical Scien
- Division Of Materials Research [820054] Funding Source: National Science Foundation
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Actomyosin contractility is essential for biological force generation, and is well understood in highly organized structures such as striated muscle. Additionally, actomyosin bundles devoid of this organization are known to contract both in vivo and in vitro, which cannot be described by standard muscle models. To narrow down the search for possible contraction mechanisms in these systems, we investigate their microscopic symmetries. We show that contractile behavior requires non-identical motors that generate large-enough forces to probe the nonlinear elastic behavior of F-actin. This suggests a role for filament buckling in the contraction of these bundles, consistent with recent experimental results on reconstituted actomyosin bundles.
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