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In-silico folding of a three helix protein and characterization of its free-energy landscape in an all-atom forcefield

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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 forcefield. Six of twenty simulations using an adapted basin-hopping method converged to better than 3 Åbackbone 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.
5 pages 3 figures, high quality color figures available by request

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Biological Physics, Computational Physics, Biomolecules

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