Abstract
Based on available experimental data and using a theoretical model of protein folding, we demonstrate that there is an optimal ratio between the average conformational entropy and the average contact energy per residue for fast protein folding. A statistical analysis of the conformational entropy and the number of contacts per residue for 5829 protein domains from four main classes (α, β, α/β, α+β) shows that each class has its own characteristic average number of contacts per residue and average conformational entropy per residue. These class-specific characteristics determine the protein folding rates: α-proteins are the fastest to fold, β-proteins are the second fastest, α+β-proteins are the third, and α/β-proteins are the last to fold.
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Original Russian Text © O.V. Galzitskaya, S.A. Garbuzinskii, 2006, published in Biofizika, 2006, Vol. 51, No. 4, pp. 622–632.
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Galzitskaya, O.V., Garbuzinskii, S.A. Optimal ratio between the average conformational entropy and the average energy of interaction between residues for fast protein folding. BIOPHYSICS 51, 554–564 (2006). https://doi.org/10.1134/S0006350906040075
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DOI: https://doi.org/10.1134/S0006350906040075