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

dc.creator	Herges, T.
dc.creator	Wenzel, W.
dc.date	2003-10-29
dc.date.accessioned	2026-06-02T21:40:31Z
dc.description	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.
dc.description	5 pages 3 figures, high quality color figures available by request
dc.identifier	https://arxiv.org/abs/physics/0310146
dc.identifier	http://arxiv.org/abs/physics/0310146
dc.identifier.uri	https://demo.dspace.org/handle/10673/1637
dc.subject	Biological Physics
dc.subject	Computational Physics
dc.subject	Biomolecules
dc.title	In-silico folding of a three helix protein and characterization of its free-energy landscape in an all-atom forcefield
dc.type	text

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