dorsal/arxiv
View SchemaSimple Mechanical Equivalents of Stepping Rotary Dynamics in F$_1$-ATPase
| Authors | A. V. Zolotaryuk, V. N. Ermakov, P. L. Christiansen, B. Norden, Y. Zolotaryuk |
|---|---|
| Categories | |
| ArXiv ID | physics/0205005 |
| URL | https://arxiv.org/abs/physics/0205005 |
Abstract
Two simple (rotator and one-particle) mechanistic models are suggested to describe simultaneously at a minimal level of sophistication two basic functions of F$_1$-ATPase: a motor regime driven by ATP hydrolysis and its inverted function as ATP synthesis. This description is consistent with the so-called rotary binding-change mechanism, a milestone of functioning ATP synthase, and uses a stepping (driving) function associated with two sequences of time instants, at which hydrolysis and synthesis reactions occur. It is useful to analyse experimental data and numerical simulations indeed predict corresponding dynamic behavior.
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"abstract": "Two simple (rotator and one-particle) mechanistic models are suggested to\ndescribe simultaneously at a minimal level of sophistication two basic\nfunctions of F$_1$-ATPase: a motor regime driven by ATP hydrolysis and its\ninverted function as ATP synthesis. This description is consistent with the\nso-called rotary binding-change mechanism, a milestone of functioning ATP\nsynthase, and uses a stepping (driving) function associated with two sequences\nof time instants, at which hydrolysis and synthesis reactions occur. It is\nuseful to analyse experimental data and numerical simulations indeed predict\ncorresponding dynamic behavior.",
"arxiv_id": "physics/0205005",
"authors": [
"A. V. Zolotaryuk",
"V. N. Ermakov",
"P. L. Christiansen",
"B. Norden",
"Y. Zolotaryuk"
],
"categories": [
"physics.bio-ph",
"q-bio"
],
"title": "Simple Mechanical Equivalents of Stepping Rotary Dynamics in F$_1$-ATPase",
"url": "https://arxiv.org/abs/physics/0205005"
},
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