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Title: Self-organized critical model for protein folding
Other Titles: Physica A
Authors: Moret, M.A.
Keywords: Tsallis statistics;Mass-size exponent;Solvent accessible surface area;Self-organized criticality;Scaling
Issue Date: 2011
Citation: Moret, M.A.. Self-organized critical model for protein folding. Physica. A (Print), v. 390, p. 3055-3059, 2011.
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. ©
Description: p.3055-3059
Appears in Collections:Artigos Publicados em Periódicos (PPG MCTI)

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