Theory of protein molecule self-organization. III. A calculating method for the probabilities of the secondary structure formation in an unfolded polypeptide chain |
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Authors: | A. V. Finkelstein |
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Abstract: | A mathematical model is developed adequately describing an unfolded polypeptide chain without long-range interactions in which fluctuating hydrogen-bonded α-helices, β-bends, fragments of helices 310, and other local structures are formed. The obtained model is a modification of a one-dimensional Ising model for a heteropolymer and allows one to determine the probability of formation of different secondary structures in various parts of a polypeptide chain, provided the whole set of structural thermodynamic parameters exists. |
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