Synthesis and folding preferences of γ-amino acid oligopeptides: stereochemical control in the formation of a reverse turn and a helix
✍ Scribed by Stephen Hanessian; Xuehong Luo; Robert Schaum
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- French
- Weight
- 302 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0040-4039
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✦ Synopsis
The stereoselective synthesis of a-cinnamyl y-amino acids and the corresponding oligopeptides is described. Detailed 1D and 2D NMR studies in pyridine-ds .show that the (0tR)-cinnamyl y-amino acid tetrapeptide adopts a reverse turn structure, while the (otS)-cinnamyl y-amino acid tetrapeptide adopts a right-handed helical structure.
📜 SIMILAR VOLUMES
The analysis of the factors that control the helical folding of Aib-rich peptides is extended to include sensitivity to sequence patterns, and in particular the presence of contiguous non-Aib a-mono-alkylated residues. The distinct hydrogen-bonding network of the 310helix, as contrasted with that of
The design of nonnatural oligomers that form diversified secondary structures is an active area of research. [1] An extensive search of the b-peptide class of foldamers has provided several new secondary structures, while the gpeptides, despite the possibility of having and traversing a larger confo
The design of nonnatural oligomers that form diversified secondary structures is an active area of research. [1] An extensive search of the b-peptide class of foldamers has provided several new secondary structures, while the gpeptides, despite the possibility of having and traversing a larger confo
## Abstract The 2,2′:6′,2″‐terpyridine scaffold has been identified as a conformationally discrete structural element potentially capable of inducing reversible folding in substituents, attached through suitable spacers to its 6,6″‐positions, by metal complexation/decomplexation or by protonation/d