Abstract
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
