1UAO

NMR Structure of designed protein, Chignolin, consisting of only ten amino acids (Ensembles)

1UAO の概要

• エントリーDOI: 10.2210/pdb1uao/pdb
• 関連するPDBエントリー: 2RVD 5AWL
• NMR情報: BMRB: 5694
• 分子名称: Chignolin (1 entity in total)
• 機能のキーワード: de novo protein, beta-hairpin, mini-protein, g-peptide, autonomous element
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1082.08

構造登録者

Honda, S.,Yamasaki, K. (登録日: 2003-03-13, 公開日: 2004-04-13, 最終更新日: 2023-12-27)

主引用文献

Honda, S.,Yamasaki, K.,Sawada, Y.,Morii, H.
10 residue folded peptide designed by segment statistics
Structure, 12:1507-1518, 2004

PubMed Abstract: We have designed a peptide termed chignolin, consisting of only 10 amino acid residues (GYDPETGTWG), on the basis of statistics derived from more than 10,000 protein segments. The peptide folds into a unique structure in water and shows a cooperative thermal transition, both of which may be hallmarks of a protein. Also, the experimentally determined beta-hairpin structure was very close to what we had targeted. The performance of the short peptide not only implies that the methodology employed here can contribute toward development of novel techniques for protein design, but it also yields insights into the raison d'etre of an autonomous element involved in a natural protein. This is of interest for the pursuit of folding mechanisms and evolutionary processes of proteins.

PubMed: 15296744
DOI: 10.1016/j.str.2004.05.022

実験手法

SOLUTION NMR