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