Scaling and self-organized criticality in proteins II.
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.
Phillips
J C
JC
Department of Physics and Astronomy, Rutgers University, Piscataway, NJ 08854, USA. jcphillips8@comcast.net
D002467:Cell Nucleus / Q000737:chemistry / Q000378:metabolism; D003593:Cytoplasm / Q000737:chemistry / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D021381:Protein Transport; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D055672:Static Electricity
D011506:Proteins