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Hydrogen bonding in peptide helices Analysis of two independent helices in the crystal structure of a peptide Boc-Val-Ala-Leu-Aib-Val-Ala-Phe-OMe

✍ Scribed by DATTA, SAUMEN ;SHAMALA, N. ;BANERJEE, ARINDAM ;BALARAM, P.

Book ID
110893593
Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
547 KB
Volume
49
Category
Article
ISSN
1397-002X

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📜 SIMILAR VOLUMES

Helix aggregation in peptide crystals: O
Helix aggregation in peptide crystals: Occurrence of either all parallel or antiparallel packing motifs for α-helices in polymorphs of Boc-Aib-Ala-Leu-Ala-Leu-Aib-Leu-Ala-Leu-Aib-OMe
✍ Isabella L. Karle; Judith L. Flippen-Anderson; K. Uma; P. Balaram 📂 Article 📅 1990 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 722 KB

Leu-Ala-Leu-Aib-OMe, have been obtained. Antiparallel helix aggregation is observed in crystals grown from methanol ( A ) , while completely parallel packing is observed in crystals from isopropanol ( B ) or an ethylene glycol-ethanol mixture ( C ) . Crystals B and C are very similar in molecular co

Stabilization of unusual structures in p
Stabilization of unusual structures in peptides using α,β-dehydrophenylalanine: Crystal and solution structures of Boc–Pro–ΔPhe–Val–ΔPhe–Ala–OMe and Boc–Pro–ΔPhe–Gly–ΔPhe–Ala–OMe
✍ Puniti Mathur; U. A. Ramagopal; S. Ramakumar; N. R. Jagannathan; V. S. Chauhan 📂 Article 📅 2006 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 408 KB 👁 1 views

## Abstract The structures of two dehydropentapeptides, Boc–Pro–ΔPhe–Val–ΔPhe–Ala–OMe (**I**) and Boc–Pro–ΔPhe–Gly–ΔPhe–Ala–OMe (**II**) (Boc: __t__‐butoxycarbonyl), have been determined by nuclear magnetic resonance (NMR), circular dichroism (CD), and X‐ray crystallographic studies. The peptide **

Role of a two-residue spacer in an α,β-d
Role of a two-residue spacer in an α,β-didehydrophenylalanine containing hexapeptide: crystal and solution structure of Boc-Val-ΔPhe-Leu-Ala-ΔPhe-Ala-OMe
✍ Anil K. Padyana; S. Ramakumar; Puniti Mathur; N. R. Jagannathan; V. S. Chauhan 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 152 KB

## Abstract The peptide Boc‐Val^1^‐ΔPhe^2^‐Leu^3^‐Ala^4^‐ΔPhe^5^‐Ala^6^‐OMe has been examined for the structural consequence of placing a two‐residue segment between the ΔPhe residues. The peptide is stabilized by four consecutive β‐turns. The overall conformation of the molecule is a right‐handed