Ultrafast folding of a computationally designed Trp-cage mutant: Trp2-cage.
Miniproteins provide useful model systems for understanding the principles of protein folding and design. These proteins also serve as useful test cases for theories of protein folding, and their small size and ultrafast folding kinetics put them in a regime of size and time scales that is now becoming accessible to molecular dynamics simulations. Previous estimates have suggested the "speed limit" for folding is on the order of 1 mus. Here a computationally designed mutant of the 20-residue Trp-cage miniprotein, Trp2-cage, is presented. The Trp2-cage has greater stability than the parent and folds on the ultrafast time scale of 1 mICROs at room temperature, as determined from infrared temperature-jump experiments.
Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Michelle R
MR
Bunagan
Xi
X
Yang
Jeffery G
JG
Saven
Feng
F
Gai
D003198:Computer Simulation; D006860:Hydrogen Bonding; D007700:Kinetics; D009154:Mutation; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
D010455:Peptides; C508725:Trp-cage peptide