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On the two kinds of nucleation in the helix–coil transition theory of polypeptide chains
Author(s) -
Bixon M.,
Lifson S.
Publication year - 1967
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.1967.360050605
Subject(s) - nucleation , chemistry , partition function (quantum field theory) , random coil , helix (gastropod) , sequence (biology) , partition (number theory) , crystallography , molecule , chemical physics , physics , quantum mechanics , mathematics , combinatorics , circular dichroism , ecology , biochemistry , organic chemistry , snail , biology
The nucleation of a helical sequence from a random chain of the polypeptide molecule as well as the nucleation of a random‐coil sequence from the helical conformation of the molecule are considered simultaneously in evaluating the partition function of the system. This partition function is then used for a comparative analysis of the theories of Zimm and Bragg, Gibbs and DiMarzio, and Lifson and Roig. It is shown that while all three account properly for the essential nature of the nucleation phenomenon the first considers in detail the random‐coil nucleation, the second emphasizes the details of the helix nucleation, while the third neglects the fine details of both in a symmetric way.