ArticleProceedings of the National Academy of Sciences of the United States of America2009
Scaling and self-organized criticality in proteins I.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Learning molecular traits of human pain disease via voltage-gated sodium channel structure renormalization.Computational and structural biotechnology journal · 2025Article
- Folding-unfolding asymmetry and aRoyal Society open science · 2023Article
- Topological bio-scaling analysis as a universal measure of protein folding.Royal Society open science · 2022Article
- Relating SARS-CoV-2 variants using cellular automata imaging.Scientific reports · 2022Article
- Hydropathicity-based prediction of pain-causing NaV1.7 variants.BMC bioinformatics · 2021Article
- Non-extensitivity and criticality of atomic hydropathicity around a voltage-gated sodium channel's pore: a modeling study.Journal of biological physics · 2021Article
- Survival of Virus Particles in Water Droplets: Hydrophobic Forces and Landauer's Principle.Entropy (Basel, Switzerland) · 2021Article
- Long-range correlation in protein dynamics: Confirmation by structural data and normal mode analysis.PLoS computational biology · 2020Article
- From superhydrophobicity to icephobicity: forces and interaction analysis.Scientific reports · 2013Article
- Article
- Scaling and self-organized criticality in proteins II.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Scaling and self-organized criticality in proteins I.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Article
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1 author.
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Abstract
The complexity of proteins is substantially simplified by regarding them as archetypical examples of self-organized criticality (SOC). To test this idea and elaborate on it, this article applies the Moret-Zebende SOC hydrophobicity scale to the large-scale scaffold repeat protein of the HEAT superfamily, PR65/A. Hydrophobic plasticity is defined and used to identify docking platforms and hinges from repeat sequences alone. The difference between the MZ scale and conventional hydrophobicity scales reflects long-range conformational forces that are central to protein functionality.
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