Premium
Crystal structure of a tripeptide, L ‐alanyl‐glycyl‐glycine and its relevance to the poly(glycine)‐II type of conformation
Author(s) -
Subramanian E.,
Lalitha V.
Publication year - 1983
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.360220306
Subject(s) - tripeptide , glycine , chemistry , intermolecular force , hydrogen bond , molecule , stereochemistry , crystallography , helix (gastropod) , crystal structure , amino acid , biochemistry , organic chemistry , ecology , snail , biology
A tripeptide molecule, L ‐alanyl‐glycyl‐glycine, crystallizes in the form of a left‐handed helix with (ϕ,ψ) = −83°, 170°. A pseudohexagonal packing arrangement and interchain hydrogen‐bonded interactions are reminiscent of the model for the structure of poly(glycine)‐II. Observations of certain intermolecular interactions appear to be relevant to the stereochemical assumptions incorporated in the models proposed for poly(glycine)‐II and related polypeptides.