## 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
β-Turn conformations in crystal structures of model peptides containing α,α-Di-n-propylglycine and α,α-Di-n-butylglycine
✍ Scribed by M. Crisma; G. Valle; C. Toniolo; Sudhanand Prasad; R. Balaji Rao; P. Balaram
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1995
- Tongue
- English
- Weight
- 515 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0006-3525
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Some theoretical studies have predicted that the conformational freedom of the cy-aminoisobutyric acid (H-Aib-OH) residue is restricted to the a-helical region of the Ramachandran map. In order to obtain conformational experimental data, two model peptide derivatives, MeCO-Aib-NHMe 1 and Bu'CO-LPro-
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## Abstract The crystal structures of two helical peptides Boc‐Val‐Ala‐Leu‐Aib‐Val‐Ala‐Leu‐OMe (VALU‐7) and Boc‐Val‐Ala‐Leu‐Aib‐Val‐Ala‐Leu‐Aib‐OMe (VALU‐8) have been determined to a resolution of 1.0 and 0.9 Å, respectively. Both the seven and eight residue peptides crystallize with two conformers