Statistical mechanics of noncovalent bonds in polyamino acids. III. Interhelical hydrophobic bonds in short chains | Zendy

Poland Douglas C. | Zendy; Scheraga Harold A. | Zendy

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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.

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