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| Autores principales: | , , , |
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| Formato: | Preprint |
| Publicado: |
2024
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| Materias: | |
| Acceso en línea: | https://arxiv.org/abs/2411.02340 |
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| _version_ | 1866915004574334976 |
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| author | McGrath, Jake Kent, Brian Johnson, Colin Alvarado, José |
| author_facet | McGrath, Jake Kent, Brian Johnson, Colin Alvarado, José |
| contents | Myosin motors are fundamental biological actuators, powering diverse mechanical tasks in eukaryotic cells via ATP hydrolysis. Recent work revealed that myosin's velocity-dependent detachment rate can bridge actomyosin dynamics to macroscale Hill muscle predictions. However, the influence of this microscale unbinding, which we characterize by a dimensionless parameter $α$, on macroscale energetic flows-such as power consumption, output and efficiency-remains elusive. Here we develop an analytical model of myosin dynamics that relates unbinding rates $α$ to energetics. Our model agrees with published in-vivo muscle data and, furthermore, uncovers a performance-efficiency tradeoff governed by $α$. To experimentally validate the tradeoff, we build HillBot, a robophysical model of Hill's muscle that mimics nonlinearity. Through HillBot, we decouple $α$'s concurrent effect on performance and efficiency, demonstrating that nonlinearity drives efficiency. We compile 136 published measurements of $α$ in muscle and myoblasts to reveal a distribution centered at $α^* = 3.85 \pm 2.32$. Synthesizing data from our model and HillBot, we quantitatively show that $α^*$ corresponds to a class of generalist actuators that are both relatively powerful and efficient, suggesting that the performance-efficiency tradeoff underpins the prevalence of $α^*$ in nature. We leverage these insights and propose a nonlinear variable-impedance protocol to shift along a performance-efficiency axis in robotic applications. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2411_02340 |
| institution | arXiv |
| publishDate | 2024 |
| record_format | arxiv |
| spellingShingle | Microscale velocity-dependent unbinding generates a macroscale performance-efficiency tradeoff in actomyosin systems McGrath, Jake Kent, Brian Johnson, Colin Alvarado, José Biological Physics Myosin motors are fundamental biological actuators, powering diverse mechanical tasks in eukaryotic cells via ATP hydrolysis. Recent work revealed that myosin's velocity-dependent detachment rate can bridge actomyosin dynamics to macroscale Hill muscle predictions. However, the influence of this microscale unbinding, which we characterize by a dimensionless parameter $α$, on macroscale energetic flows-such as power consumption, output and efficiency-remains elusive. Here we develop an analytical model of myosin dynamics that relates unbinding rates $α$ to energetics. Our model agrees with published in-vivo muscle data and, furthermore, uncovers a performance-efficiency tradeoff governed by $α$. To experimentally validate the tradeoff, we build HillBot, a robophysical model of Hill's muscle that mimics nonlinearity. Through HillBot, we decouple $α$'s concurrent effect on performance and efficiency, demonstrating that nonlinearity drives efficiency. We compile 136 published measurements of $α$ in muscle and myoblasts to reveal a distribution centered at $α^* = 3.85 \pm 2.32$. Synthesizing data from our model and HillBot, we quantitatively show that $α^*$ corresponds to a class of generalist actuators that are both relatively powerful and efficient, suggesting that the performance-efficiency tradeoff underpins the prevalence of $α^*$ in nature. We leverage these insights and propose a nonlinear variable-impedance protocol to shift along a performance-efficiency axis in robotic applications. |
| title | Microscale velocity-dependent unbinding generates a macroscale performance-efficiency tradeoff in actomyosin systems |
| topic | Biological Physics |
| url | https://arxiv.org/abs/2411.02340 |