1R9V

NMR Structure of a D,L-Alternating Dodecamer of Norleucine

1R9V の概要

• エントリーDOI: 10.2210/pdb1r9v/pdb
• NMR情報: BMRB: 6039
• 関連するBIRD辞書のPRD_ID: PRD_000106
• 分子名称: BOC-(D-NLE-L-NLE)4-D-NLE(METHYL)-L-NLE-D-NLE-L-NLE METHYL ESTER (1 entity in total)
• 機能のキーワード: beta helix, ion channel, de novo protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1504.08

構造登録者

Navarro, E.,Celda, B. (登録日: 2003-10-31, 公開日: 2003-12-02, 最終更新日: 2023-11-15)

主引用文献

Navarro, E.,Tejero, R.,Fenude, E.,Celda, B.
Solution NMR Structure of a D,L-Alternating Oligonorleucine as a Model of Beta-Helix
Biopolymers, 59:110-119, 2001

PubMed Abstract: beta-Helix structures are of particular interest due to their capacity to form transmembrane channels with different transport properties. However, the relatively large number of beta-helices configurations does not allow a direct conformational analysis of beta-helical oligopeptides. A synthetic alternating D,L-oligopeptide with twelve norleucines (XIIMe) has been used as a model to get insight in the conformational features of beta-helix structures. The spatial configuration of XIIMe in solution has been determined by NMR. An extensive set of distances (nuclear Overhauser effect) and dihedral (J coupling constants) constraints have been included in molecular dynamics calculations. The NMR experimental data and theoretical calculations clearly indicate that the XIIMe adopts a single beta(4.4)-helix-type conformation in nonpolar solvents.

PubMed: 11373724
DOI: 10.1002/1097-0282(200108)59:2<110::AID-BIP1010>3.3.CO;2-J

実験手法

SOLUTION NMR