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On the Statistical Mechanical Theories of Helix‐Coil Transition in Polypeptides, and the Structure and Structural Stability of Proteins
Author(s) -
Lifson S.,
Lotan N.
Publication year - 1974
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.197400019
Subject(s) - chemistry , cooperativity , random coil , helix (gastropod) , protein stability , transition (genetics) , nucleation , sequence (biology) , protein design , protein structure , crystallography , chemical physics , biophysics , circular dichroism , biochemistry , ecology , organic chemistry , snail , gene , biology
The theoretical and experimental study of the helix‐coil transition of synthetic polypeptides has significantly deepened our understanding of the phenomena of nucleation and cooperativity in the equilibrium transition between the native and the denatured states of proteins. Proteins differ, however, from synthetic copolymers by being neither regular nor random, their sequence having been determined by natural selection. Therefore, the quantitative results of the theoretical analysis of synthetic polypeptides should not be indiscriminately transferred to the study of proteins. However, these results provide important information for a rational analysis of the conformation and conformational stability of proteins.