Scaling Law for Radius of Gyration and Its Dependence on Hydrophobicity

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dc.creatorHong, Liu
dc.creatorLei, Jinzhi
dc.date2007-11-23
dc.date.accessioned2026-07-07T08:44:38Z
dc.date.available2026-07-07T08:44:38Z
dc.descriptionScaling law for geometrical and dynamical quantities of biological molecules is an interesting topic. According to Flory's theory, a power law between radius of gyration and the length of homopolymer chain is found, with exponent 3/5 for good solvent and 1/3 for poor solvent. For protein in physiological condition, a solvent condition in between, a power law with exponent ~2/5 is obtained. In this paper, we present a unified formula to cover all above cases. It shows that the scaling exponents are generally correlated with fractal dimension of a chain under certain solvent condition. While applying our formula to protein, the fractal dimension is found to depend on its hydrophobicity. By turning a physical process-varying hydrophobicity of a chain by amino acid mutation, to an equivalent chemical process-varying polarity of solvent by adding polar or nonpolar molecules, we successfully deprive this relation, with reasonable agreement to statistical data. And it will be helpful for protein structure prediction. Our results indicate that the protein may share the same basic principle with homopolymer, despite its specificity as a heteropolymer.
dc.description7 pages, 8 figures
dc.identifierhttps://arxiv.org/abs/0711.3679
dc.identifierhttp://arxiv.org/abs/0711.3679
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/142725
dc.subjectBiological Physics
dc.subjectChemical Physics
dc.titleScaling Law for Radius of Gyration and Its Dependence on Hydrophobicity
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