 Clustering structures of large proteins using multifractal analyses based on a 6-letter model and hydrophobicity scale of amino acidsJian-Yi Yang, Zu-Guo Yu and Vo Anh Chaos, Solitons & Fractals, 2009, vol. 40, issue 2, 607-620 Abstract: The Schneider and Wrede hydrophobicity scale of amino acids and the 6-letter model of protein are proposed to study the relationship between the primary structure and the secondary structural classification of proteins. Two kinds of multifractal analyses are performed on the two measures obtained from these two kinds of data on large proteins. Nine parameters from the multifractal analyses are considered to construct the parameter spaces. Each protein is represented by one point in these spaces. A procedure is proposed to separate large proteins in the α, β, α+β and α/β structural classes in these parameter spaces. Fisher’s linear discriminant algorithm is used to assess our clustering accuracy on the 49 selected large proteins. Numerical results indicate that the discriminant accuracies are satisfactory. In particular, they reach 100.00% and 84.21% in separating the α proteins from the {β,α+β,α/β} proteins in a parameter space; 92.86% and 86.96% in separating the β proteins from the {α+β,α/β} proteins in another parameter space; 91.67% and 83.33% in separating the α/β proteins from the α+β proteins in the last parameter space. Date: 2009 Downloads: (external link) Related works: Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text Persistent link: https://EconPapers.repec.org/RePEc:eee:chsofr:v:40:y:2009:i:2:p:607-620 DOI: 10.1016/j.chaos.2007.08.014 Access Statistics for this article Chaos, Solitons & Fractals is currently edited by Stefano Boccaletti and Stelios Bekiros More articles in Chaos, Solitons & Fractals from Elsevier |
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