5HG2
Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-2-Asn35
5HG2 の概要
| エントリーDOI | 10.2210/pdb5hg2/pdb |
| 関連するPDBエントリー | 5HFY 5HI1 |
| 分子名称 | Immunoglobulin G-binding protein G, GLYCEROL, MAGNESIUM ION, ... (4 entities in total) |
| 機能のキーワード | synthetic protein, de novo protein |
| 由来する生物種 | Streptococcus sp. group G |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 25343.78 |
| 構造登録者 | Tavenor, N.A.,Reinert, Z.E.,Lengyel, G.A.,Griffith, B.D.,Horne, W.S. (登録日: 2016-01-07, 公開日: 2016-02-24, 最終更新日: 2023-11-15) |
| 主引用文献 | Tavenor, N.A.,Reinert, Z.E.,Lengyel, G.A.,Griffith, B.D.,Horne, W.S. Comparison of design strategies for alpha-helix backbone modification in a protein tertiary fold. Chem.Commun.(Camb.), 52:3789-3792, 2016 Cited by PubMed Abstract: We report here the comparison of five classes of unnatural amino acid building blocks for their ability to be accommodated into an α-helix in a protein tertiary fold context. High-resolution structural characterization and analysis of folding thermodynamics yield new insights into the relationship between backbone composition and folding energetics in α-helix mimetics and suggest refined design rules for engineering the backbones of natural sequences. PubMed: 26853882DOI: 10.1039/c6cc00273k 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






