Self-organized critical model for protein folding

M.A. Moret

Physica A: Statistical Mechanics and its Applications, 2011, vol. 390, issue 17, 3055-3059

Abstract: The major factor that drives a protein toward collapse and folding is the hydrophobic effect. At the folding process a hydrophobic core is shielded by the solvent-accessible surface area of the protein. We study the fractal behavior of 5526 protein structures present in the Brookhaven Protein Data Bank. Power laws of protein mass, volume and solvent-accessible surface area are measured independently. The present findings indicate that self-organized criticality is an alternative explanation for the protein folding. Also we note that the protein packing is an independent and constant value because the self-similar behavior of the volumes and protein masses have the same fractal dimension. This power law guarantees that a protein is a complex system. From the analyzed data, q-Gaussian distributions seem to fit well this class of systems.

Keywords: Tsallis statistics; Mass-size exponent; Solvent accessible surface area; Self-organized criticality; Scaling (search for similar items in EconPapers)
Date: 2011
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Citations: View citations in EconPapers (2)

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Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:390:y:2011:i:17:p:3055-3059

DOI: 10.1016/j.physa.2011.04.008

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