Scaling and self-organized criticality in proteins II.
basic_science · Level V
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- Record sourced from PubMed, PMID 19124778.
- Also identified by DOI 10.1073/pnas.0811308105 and PMC identifier 2651307.
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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 to elaborate it, this article applies the Moret-Zebende (MZ) SOC hydrophobicity scale to transport repeat proteins of the HEAT superfamily, importin beta, and transportin, as well as the export protein Cse1p, and their ubiquitous cargo manager Ran. The difference between the MZ scale and conventional hydrophobicity scales reflects long-range conformational forces that are central to protein functionality. These compete with long-range Coulomb forces associated with cationic and anionic side chains in a revealing way.
Medical subject headings
- Proteins