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Animal skeletal muscle exhibits very interesting behavior at near-stall forces (when the muscle is loaded so strongly that it can barely contract). Near this physical limit, the actin-myosin cross bridges do more work than their energy releasing molecules, Adenosine TriPhosphate (ATP) suggest they can. It has been shown that the advantageous utilization of thermal agitation is a likely source for this increased capacity. Here, we propose a spatially two-dimensional mechanical model to illustrate how thermal agitation can be harvested for useful mechanical work in molecular machinery inspired by this biomechanical phenomenon without rate functions or empirically-inspired spatial potential functions. Additionally, the model accommodates variable lattice spacing, and it paves the way for a full three dimensional model of cross-bridge interactions where myosin II may be azimuthally misaligned with actin binding sites. With potential energy sources based entirely on realizable components, this model lends itself to the design of artificial, molecular-scale motors.
This article was published in the following journal.
Name: Journal of biomechanical engineering
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