Phys. Rev. Lett. 94, 018101 (2005) [4 pages]In Silico Folding of a Three Helix Protein and Characterization of Its Free-Energy Landscape in an All-Atom Force FieldReceived 29 October 2003; published 5 January 2005 We report the reproducible first-principles folding of the 40 amino-acid, three-helix headpiece of the HIV accessory protein in a recently developed all-atom free-energy force field. Six of 20 simulations using an adapted basin-hopping method converged to better than 3 Å backbone rms deviation to the experimental structure. Using over 60 000 low-energy conformations of this protein, we constructed a decoy tree that completely characterizes its folding funnel. © 2005 The American Physical Society URL:
http://link.aps.org/doi/10.1103/PhysRevLett.94.018101
DOI:
10.1103/PhysRevLett.94.018101
PACS:
87.15.Cc, 02.60.Pn, 02.70.Ns
|
|
About | Terms and Conditions | Subscriptions | Search | Help
Use of the American Physical Society websites and journals implies that the user has read and agrees to our Terms and Conditions and any applicable Subscription Agreement. Physical Review®, Physical Review Letters®, Reviews of Modern Physics®, and Physical Review Special Topics® are trademarks of the American Physical Society.