title: Scaling and self-organized criticality in proteins I.
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.
authors.affiliation: Department of Physics and Astronomy, Rutgers University, Piscataway, NJ 08854, USA. jcphillips8@comcast.net
authors.forename: J C
authors.initials: JC
authors.lastname: Phillips
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins