The role of the amino acid proline in influencing the secondary and tertiary structure of proteins and polypeptides has been an area of active study for many years. We have investigated this problem by incorporating the four-membered ring amino acid, azetidine-2carboxylic acid, into some proline pol
Synthesis and circular dichroism characterization of L-azetidine-2-carboxylic acid cyclic peptides
โ Scribed by R. Boni; A. S. Verdini; C. M. Deber; E. R. Blout
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1978
- Tongue
- English
- Weight
- 586 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-3525
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โฆ Synopsis
Several cyclic homopeptides containing ~-azetidine-2-carhoxylic acid (Aze)-an imino acid homologous with proline but containing one less methylene group in its cyclic side chain-have been prepared. T h e peptides reported include cyclo(Aze)e, cyclo(Aze):$, and cyclo(Aze),j. T h e synthesis and spectral characterization of these cyclic peptides are described, and the results discussed in terms o f the rigidity and steric constraints attributahle to Azecontaining peptides. CD spectra of these materials in several solvents are reported and compared with those of proline analogs; the similarity between the CD spectra of'cyclo(Aze):% and cyclo(Pro):I is noted.
* This is paper XX of the series "Cyclic Peptides." For the previous paper in this series.
๐ SIMILAR VOLUMES
Two mutant Chinese hamster lung fibroblast lines have been isolated that are resistant to the the toxic proline analog L-azetidine-2-carboxylic acid. The line designated AZCA-1 has 30-fold elevated activity of pyrroline-5-carboxylate synthase and a large increase in the rate of proline production an
## Abstract The alteration of polymer conformational properties caused by the replacement of Lโproline by Lโazetidineโ2โcarboxylic acid (Aze) has been studied by means of conformational energy computations. In addition to poly (Aze), two sequential copolymers, poly (ProโAze) and poly(Aze~3~โPro~3~)