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The effect of the L ‐azetidine‐2‐carboxylic acid residue on protein conformation. III. Collagen‐like poly(tripeptide)s
Author(s) -
Zagari Adriana,
Némethy George,
Scheraga Harold A.
Publication year - 1990
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.360300911
Subject(s) - chemistry , tripeptide , residue (chemistry) , azetidine , carboxylic acid , stereochemistry , amino acid residue , peptide , biochemistry , peptide sequence , gene
The chemical and biological properties of collagen are altered by the biosynthetic substitution of the L ‐azetidine‐2‐carboxylic acid (Aze) residue in the place of proline. The reasons for this alteration have been studied by means of conformational energy computations on single‐ and triple‐stranded structures formed by poly (GIy‐X‐Y) poly(tripeptide)s, where X and Y can be Pro or Aze. The most stable triple helix formed by Poly (Gly‐Pro‐Aze) is collagen‐like, but all low‐energy triple helices that can be formed by poly (Gly‐Aze‐Pro) and poly (Gly‐Aze‐Aze) are very different from collagen. Thus, the regular substitution of Aze for Pro in position X is not compatible with the collagen structure. In the absence of solvent effects, all of these triple helices are stable, relative to the statistical coil, but the substitutions reduce the stability of the collagen‐like triple helix, as compared with poly (Gly‐Pro‐Pro).