The chemical and biological properties of collagen are altered by the biosynthetic substitution of the ~-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
The effect of the L-azetidine-2-carboxylic acid residue on protein conformation. IV. Local substitutions in the collagen triple helix
✍ Scribed by Adriana Zagari; Kathleen A. Palmer; Kenneth D. Gibson; George Némethy; Harold A. Scheraga
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1994
- Tongue
- English
- Weight
- 868 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0006-3525
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## Abstract The alteration of polymer conformational properties caused by the replacement of L‐proline by L‐azetidine‐2‐carboxylic acid (Aze) has been studied by means of conformational energy computations. In addition to poly (Aze), two sequential copolymers, poly (Pro‐Aze) and poly(Aze~3~‐Pro~3~)
## Abstract The L‐azetidine‐2‐carboxylic acid (Aze) residue can be incorporated into proteins in the place of L‐proline, of which it is the lower homologue. This substitution alters the properties of proteins, especially of collagen. Conformational constraints in N‐acetyl‐Aze‐N′‐methylamide and in