Scaling laws in simple and complex proteins: Size scaling effects associated with domain number and folding class

DOI10.1007/S10910-012-0010-1MaRDI QIDQ445428zbMATH OpenOpenAlexFDO

Authors Parker Rogerson, Gustavo A. Arteca

Publication date 24 August 2012

Published in Journal of Mathematical Chemistry (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1007/s10910-012-0010-1

zbMATH Keywords

Folding familiesPolymer sizeProtein domainsProtein foldsSCOP data base

Mathematics Subject Classification ID

Computational methods for problems pertaining to biology (92-08) Biochemistry, molecular biology (92C40)

Recommendations

• Size scaling behaviour in protein domains belonging to the all-\(\alpha \), all-\(\beta \), \(\alpha / \beta \), and \(\alpha + \beta \) folding classes
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• Folding of proteins in Go models with angular interactions

Cites work

• Critical exponents from field theory
• Size scaling behaviour in protein domains belonging to the all-\(\alpha \), all-\(\beta \), \(\alpha / \beta \), and \(\alpha + \beta \) folding classes

Cited in

(1)

• Size scaling behaviour in protein domains belonging to the all-\(\alpha \), all-\(\beta \), \(\alpha / \beta \), and \(\alpha + \beta \) folding classes

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