ArticlePloS one2017
Minimum requirements for motility of a processive motor protein.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Motor guidance by long-range communication on the microtubule highway.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Modeling spatiotemporally varying protein-protein interactions in CyLaKS, the Cytoskeleton Lattice-based Kinetic Simulator.The European physical journal. E, Soft matter · 2021Article
- From isolated structures to continuous networks: A categorization of cytoskeleton-based motile engineered biological microstructures.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2019Review
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Motor proteins generally have a two-way coupling between the ATP hydrolysis site, the lever movement and the binding affinity for their track, which allows them to perform efficient stepping. Here we explore the minimal requirements for directed motility based on simpler schemes in which the binding/unbinding from the track is decoupled from the ATPase cycle. We show that a directed power stroke alone is not sufficient for motility, but combined with an asymmetry in force-induced unbinding rates it can generate stepping. The energetic efficiency of such stepping is limited to approximately 20%. We conclude that the allosteric coupling between the ATP hydrolysis and the track binding is not strictly necessary for motility, but it greatly improves its efficiency.
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