ArticleProceedings of the National Academy of Sciences of the United States of America2020
Self-organized networks: Darwinian evolution of dynein rings, stalks, and stalk heads.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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6 citing papers in PubMed, 14 citations in OpenAlex.
- The Statistical Trends of Protein Evolution: A Lesson from AlphaFold Database.Molecular biology and evolution · 2022Article
- Phase transitions may explain why SARS-CoV-2 spreads so fast and why new variants are spreading faster.Physica A · 2022Article
- Darwinian Evolution of Intelligence.Frontiers in bioinformatics · 2022Article
- Synchronized attachment and the Darwinian evolution of coronaviruses CoV-1 and CoV-2.Physica A · 2021Article
- Reply to Koonin et al.: Evolution of proteins is Darwinian.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- No waves of intelligent design.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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1 author at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Cytoskeletons are self-organized networks based on polymerized proteins: actin, tubulin, and driven by motor proteins, such as myosin, kinesin, and dynein. Their positive Darwinian evolution enables them to approach optimized functionality (self-organized criticality). Dynein has three distinct titled subunits, but how these units connect to function as a molecular motor is mysterious. Dynein binds to tubulin through two coiled coil stalks and a stalk head. The energy used to alter the head binding and propel cargo along tubulin is supplied by ATP at a ring 1,500 amino acids away. Here, we show how many details of this extremely distant interaction are explained by water waves quantified by thermodynamic scaling. Water waves have shaped all proteins throughout positive Darwinian evolution, and many aspects of long-range water-protein interactions are universal (described by self-organized criticality). Dynein water waves resembling tsunami produce nearly optimal energy transport over 1,500 amino acids along dynein's one-dimensional peptide backbone. More specifically, this paper identifies many similarities in the function and evolution of dynein compared to other cytoskeleton proteins such as actin, myosin, and tubulin.
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