1L2Y

NMR Structure of Trp-Cage Miniprotein Construct TC5b

1L2Y の概要

• エントリーDOI: 10.2210/pdb1l2y/pdb
• 関連するPDBエントリー: 1jrj
• NMR情報: BMRB: 5292
• 分子名称: TC5b (1 entity in total)
• 機能のキーワード: miniprotein, two-state folding, trp-cage, de novo protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2171.41

構造登録者

Neidigh, J.W.,Fesinmeyer, R.M.,Andersen, N.H. (登録日: 2002-02-25, 公開日: 2002-05-29, 最終更新日: 2024-05-08)

主引用文献

Neidigh, J.W.,Fesinmeyer, R.M.,Andersen, N.H.
Designing a 20-residue protein.
Nat.Struct.Biol., 9:425-430, 2002

PubMed Abstract: Truncation and mutation of a poorly folded 39-residue peptide has produced 20-residue constructs that are >95% folded in water at physiological pH. These constructs optimize a novel fold, designated as the 'Trp-cage' motif, and are significantly more stable than any other miniprotein reported to date. Folding is cooperative and hydrophobically driven by the encapsulation of a Trp side chain in a sheath of Pro rings. As the smallest protein-like construct, Trp-cage miniproteins should provide a testing ground for both experimental studies and computational simulations of protein folding and unfolding pathways. Pro Trp interactions may be a particularly effective strategy for the a priori design of self-folding peptides.

PubMed: 11979279
DOI: 10.1038/nsb798

実験手法

SOLUTION NMR