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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
Author(s) -
Finkelstein A. V.
Publication year - 1977
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1977.360160304
Subject(s) - chemistry , chain (unit) , molecule , ising model , polypeptide chain , protein secondary structure , single chain , statistical physics , thermodynamics , crystallography , chemical physics , physics , organic chemistry , biochemistry , antibody , immunology , biology , enzyme , astronomy
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.