DISTINCT FRACTAL CHARACTERISTICS OF MONOMER AND MULTIMER PROTEINS

Autor:	Adriana Isvoran, Dana Craciun, Robert D. Reisz, N. M. Avram
Rok vydání:	2010
Předmět:	Surface (mathematics) Combinatorics Folding (chemistry) chemistry.chemical_compound Monomer Fractal Chemistry Chemical physics Applied Mathematics Modeling and Simulation Surface roughness Geometry and Topology Fractal dimension
Zdroj:	Fractals. 18:207-214
ISSN:	1793-6543 0218-348X
DOI:	10.1142/s0218348x10004798
Popis:	Within this study we have calculated the surface fractal dimension (Ds) and the backbone fractal dimensions associated to the local folding (D1) and to the global folding (D2) for two unbiased sets of 50 proteins each, one for monomer and the other for homo- multimer proteins. The mean surface fractal dimension is Ds = 2.29 ± 0.02 for monomers and Ds = 2.21 ± 0.01 for multimers, the two means being significantly different. The mean backbone fractal dimensions associated to the local folding are D1 = 1.34 ± 0.14 for monomers and D1 = 1.33 ± 0.11 for multimers and those associated to the global folding are D2 = 1.33 ± 0.05 for monomers and D2 = 1.29 ± 0.04 for multimers, respectively. There are not significant differences between the mean values of the backbone fractal dimensions corresponding to monomers and multimers. These results suggest that there are different structural characteristics between monomer and multimer proteins only concerning their surface roughness, with multimers being smoother than monomers.
Databáze:	OpenAIRE
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