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Theory of protein molecule self-organization. III. A calculating method for the probabilities of the secondary structure formation in an unfolded polypeptide chain

✍ Scribed by A. V. Finkelstein


Publisher
Wiley (John Wiley & Sons)
Year
1977
Tongue
English
Weight
279 KB
Volume
16
Category
Article
ISSN
0006-3525

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✦ Synopsis


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 3~10~, 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.