Stabilisation of the type I β-turn conformation by a bicyclic analogue of proline
✍ Scribed by Ana M. Gil; Elena Buñuel; Ana I. Jiménez; Carlos Cativiela
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- French
- Weight
- 113 KB
- Volume
- 44
- Category
- Article
- ISSN
- 0040-4039
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The synthesis of the tetrapeptide benzyloxycarbonyl(a-aminoisobutyryl-L-prolyl)zmethyl ester (Z-(Aib-Pro)z-OMe) and an analysis of its conformation in solution and the solid state are reported. Stepwise synthesis using dicyclohexylcarbodiimide leads to racemization a t Pro(2). Evidence for the prese
## Abstract Designed octapeptides Boc‐Leu‐Val‐Val‐Aib‐^D^Xxx‐Leu‐Val‐Val‐OMe (^D^Xxx = ^D^Ala, 3a;^D^Val, 3c and ^D^Pro, 5a) and Boc‐Leu‐Phe‐Val‐Aib‐^D^Ala‐Leu‐Phe‐Val‐OMe (3b) have been investigated to construct models of a stable type I′ β‐turn nucleated hairpin and to generate systems for invest
## Abstract The crystal structures of two oligopeptides containing di‐n‐propylglycine (Dpg) residues, Boc‐Gly‐Dpg‐Gly‐Leu‐OMe (**1**) and Boc‐Val‐Ala‐Leu‐Dpg‐Val‐Ala‐Leu‐Val‐Ala‐Leu‐Dpg‐Val‐Ala‐Leu‐OMe (**2**) are presented. Peptide **1** adopts a type I′β‐turn conformation with Dpg(2)–Gly(3) at th
## Abstract Previous studies have indicated that proteolytic activation of pro‐hormones and pro‐proteins occurs most frequently at the level of basic amino acids arranged in doublets and that the dibasic sites are situated in or next to __β__‐turns. Investigations utilizing synthetic peptides repro