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

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dc.creatorHerges, T.
dc.creatorWenzel, W.
dc.date2003-10-29
dc.date.accessioned2026-07-07T05:50:21Z
dc.date.available2026-07-07T05:50:21Z
dc.descriptionWe 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.
dc.description5 pages 3 figures, high quality color figures available by request
dc.identifierhttps://arxiv.org/abs/physics/0310146
dc.identifierhttp://arxiv.org/abs/physics/0310146
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/85686
dc.subjectBiological Physics
dc.subjectComputational Physics
dc.subjectBiomolecules
dc.titleIn-silico folding of a three helix protein and characterization of its free-energy landscape in an all-atom forcefield
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