10 residue folded peptide designed by segment statistics.
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.
National Institute of Advanced Industrial Science and Technology, AIST Central 6, Tsukuba 305-8566, Japan. s.honda@aist.go.jp
Shinya
S
Honda
Kazuhiko
K
Yamasaki
Yoshito
Y
Sawada
Hisayuki
H
Morii
D000465:Algorithms; D000596:Amino Acids / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding
D000596:Amino Acids; D009842:Oligopeptides; D010455:Peptides; C506175:chignolin