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Intramolecular conformational transitions “random coil–helix–folded structure” in polypeptides
Author(s) -
Adonts V. G.,
Birshtein T. M.,
Elyashevich A. M.,
Skvortsov A. M.
Publication year - 1976
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.1976.360150603
Subject(s) - intramolecular force , chemistry , random coil , helix (gastropod) , crystallography , phase diagram , macromolecule , phase transition , chemical physics , phase (matter) , stereochemistry , physics , thermodynamics , circular dichroism , ecology , biochemistry , organic chemistry , snail , biology
A general theory has been developed for conformational intramolecular transitions in a single macromolecule with a high degree of polymerization (an infinite length model) capable of forming two types of ordered structures: the α‐helix and the folded β‐structure, as well as acquiring the random coil conformation. The phase diagram analysis of this system has shown that the regular β‐structure state is separated from all other states of the chain by the phase boundary line. Any intersection of the phase boundary is a phase transition which can be either of the first order or second order, depending on values of the energy parameters of the system. Mechanisms of intramolecular rearrangements: β‐structure–random coil and α‐helix–β‐structure have been discussed. It has been shown that there exist two different mechanisms for each of these rearrangements, and the regions of parameter variation corresponding to each mechanism have been specified.