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The helix‐coil transition in polypeptides: A microscopic approach. II
Author(s) -
Hairyan Sh. A.,
Mamasakhlisov E. Sh.,
Morozov V. F.
Publication year - 1995
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.360350108
Subject(s) - cooperativity , helicity , chemistry , quantum nonlocality , degree (music) , random coil , helix (gastropod) , transition point , crystallography , thermodynamics , statistical physics , physics , quantum mechanics , circular dichroism , biochemistry , quantum entanglement , acoustics , quantum , ecology , snail , biology
Abstract In the framework of an earlier constructed model [N. S. Ananikyan et al. (1990) Biopolymers, Vol. 30. pp. 357‐367], some analytical estimates for the correlation length and degree of helicity near the transition point were obtained in the case of an arbitrary topology of hydrogen bond closing (Δ). It was shown that the Zimm‐Bragg cooperativity parameter σ is determined by the set of (Δ‐1) amino acid residues and so is nonlocal. An analytic expression for cooperatively parameters in a heteropolypeptide chain was obtained and numerical calculations showed that in case of heteropolypeptide with random primary structure the nonlocality of cooperativity parameter influenced the temperature dependence of helicity degree. © 1995 John Wiley & Sons, Inc.