A series of N-and C-protected, monodispersed homo-oligopeptides (to the dodecamer level) from the small-ring alicyclic C a,a -dialkylated glycine 1-aminocyclobutane-1-carboxylic acid (Ac 4 c) and two Ala/Ac 4 c tripeptides were synthesized by solution methods and fully characterized. The conformatio
Peptide helices with pendant cycloalkane rings. Characterization of conformations of 1-aminocyclooctane-1-carboxylic acid (Ac8c) residues in peptides
✍ Scribed by Saumen Datta; R. N. S. Rathore; S. Vijayalakshmi; Prema G. Vasudev; R. Balaji Rao; P. Balaram; Dr N. Shamala
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 285 KB
- Volume
- 10
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.507
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📜 SIMILAR VOLUMES
## Abstract The conformational preferences of the 3,3‐disubstituted β‐amino acid residue, 1‐aminocyclohexaneacetic acid (β^3,3^Ac~6~c) have been investigated by determining the crystal structures of the parent amino acid, the hydrochloride derivative, 10 protected derivatives and di and tripeptides
The author has brought to our attention the following revision for Table II of the article listed above, published in Biopolymers 2008, 90(2):138-150. See the revised table shown on the following page.
A series of N-and C-protected, monodispersed homo-oligopeptides (to the pentamer level) from the cycloaliphatic C Y -dialkylated glycine 1-aminocyclononane-1-carboxylic acid (Ac W c) and two Ala/Ac W c tripeptides have been synthesized by solution methods and fully characterized. The conformational