Abstract
Identification and study of the main principles underlying the kinetics and thermodynamics of protein folding generate a new insight into the factors that control this process. Statistical analysis of the radius of gyration for 3769 protein domains of four major classes (α, β, α/β, and α + β) showed that each class has a characteristic radius of gyration that determines the protein structure compactness. For instance, α proteins have the highest radius of gyration throughout the protein size range considered, suggesting a less tight packing as compared with β-and (α + β)-proteins. The lowest radius of gyration and, accordingly, the tightest packing are characteristic of α/β-proteins. The protein radius of gyration normalized by the radius of gyration of a ball with the same volume is independent of the protein size, in contrast to compactness and the number of contacts per residue.
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Original Russian Text © M.Yu. Lobanov, N.S. Bogatyreva, O.V. Galzitskaya, 2008, published in Molekulyarnaya Biologiya, 2008, Vol. 42, No. 4, pp. 701–706.
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Lobanov, M.Y., Bogatyreva, N.S. & Galzitskaya, O.V. Radius of gyration as an indicator of protein structure compactness. Mol Biol 42, 623–628 (2008). https://doi.org/10.1134/S0026893308040195
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DOI: https://doi.org/10.1134/S0026893308040195