Optimized Folding Simulations of Protein A

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dc.creatorTrebst, S.
dc.creatorHansmann, U. H. E.
dc.date2007-11-26
dc.date2007-12-29
dc.date.accessioned2026-07-07T09:36:34Z
dc.date.available2026-07-07T09:36:34Z
dc.descriptionWe describe optimized parallel tempering simulations of the 46-residue B-fragment of protein A. Native-like configurations with a root-mean-square deviation of approximately 3A to the experimentally determined structure (Protein Data Bank identifier 1BDD) are found. However, at biologically relevant temperatures such conformations appear with only about 10% frequency in our simulations. Possible short comings in our energy function are discussed.
dc.description6 pages, 8 figures
dc.identifierhttps://arxiv.org/abs/0711.3830
dc.identifierhttp://arxiv.org/abs/0711.3830
dc.identifierEur. Phys. J. E 24, 311 (2007).
dc.identifierdoi:10.1140/epje/i2007-10241-1
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/160163
dc.subjectStatistical Mechanics
dc.titleOptimized Folding Simulations of Protein A
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