Robust mechanobiological behavior emerges in heterogeneous myosin systems.

ABSTRACT: Biological complexity presents challenges for understanding natural phenomenon and engineering new technologies, particularly in systems with molecular heterogeneity. Such complexity is present in myosin motor protein systems, and computational modeling is essential for determining how collective myosin interactions produce emergent system behavior. We develop a computational approach for altering myosin isoform parameters and their collective organization, and support predictions with in vitro experiments of motility assays with α-actinins as molecular force sensors. The computational approach models variations in single myosin molecular structure, system organization, and force stimuli to predict system behavior for filament velocity, energy consumption, and robustness. Robustness is the

SUBMITTER: Egan PF 

PROVIDER: S-EPMC5625935 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature