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Proc Natl Acad Sci U S A. 2009 Mar 3;106(9):3113-8. doi: 10.1073/pnas.0811308105. Epub 2009 Jan 5.

Scaling and self-organized criticality in proteins II.

Author information

1
Department of Physics and Astronomy, Rutgers University, Piscataway, NJ 08854, USA. jcphillips8@comcast.net

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.

PMID:
19124778
PMCID:
PMC2651307
DOI:
10.1073/pnas.0811308105
[Indexed for MEDLINE]
Free PMC Article
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