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Statistical mechanics of noncovalent bonds in polyamino acids. III. Interhelical hydrophobic bonds in short chains
Author(s) -
Poland Douglas C.,
Scheraga Harold A.
Publication year - 1965
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.360030307
Subject(s) - chemistry , non covalent interactions , chain (unit) , hydrophobic effect , alanine , function (biology) , statistical mechanics , computational chemistry , stereochemistry , crystallography , hydrogen bond , amino acid , molecule , thermodynamics , organic chemistry , biochemistry , physics , astronomy , evolutionary biology , biology
A partition function is derived for a simple model of interacting helices in a short (20 residues) chain of poly‐ L ‐alanine. It is found that interhelical hydrophobic bonds effect a marked stabilization of helical forms, and give rise to a sharp transition of the type found in many proteins.