1UAO

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

Summary for 1UAO

• Entry DOI: 10.2210/pdb1uao/pdb
• Related: 2RVD 5AWL
• NMR Information: BMRB: 5694
• Descriptor: Chignolin (1 entity in total)
• Functional Keywords: de novo protein, beta-hairpin, mini-protein, g-peptide, autonomous element
• Total number of polymer chains: 1
• Total formula weight: 1082.08

Authors

Honda, S.,Yamasaki, K. (deposition date: 2003-03-13, release date: 2004-04-13, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

SOLUTION NMR