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dc.contributor.authorAlbrecht, A.
dc.contributor.authorSkaliotis, A.
dc.contributor.authorSteinhofel, K.
dc.date.accessioned2011-06-08T13:38:36Z
dc.date.available2011-06-08T13:38:36Z
dc.date.issued2008
dc.identifier.citationAlbrecht , A , Skaliotis , A & Steinhofel , K 2008 , ' Stochastic protein folding simulation in the three-dimensional HP-model ' , Computational Biology and Chemistry , vol. 32 , no. 4 , pp. 248-255 . https://doi.org/10.1016/j.compbiolchem.2008.03.004
dc.identifier.issn1476-9271
dc.identifier.otherPURE: 83935
dc.identifier.otherPURE UUID: b0de66e1-1b89-4816-9e05-7aaced832871
dc.identifier.otherdspace: 2299/5928
dc.identifier.otherScopus: 45549094900
dc.identifier.urihttp://hdl.handle.net/2299/5928
dc.descriptionOriginal article can be found at : http://www.sciencedirect.com/ Copyright Elsevier [Full text of this article is not available in the UHRA]
dc.description.abstractWe present results from three-dimensional protein folding simulations in the HP-model on ten benchmark problems. The simulations are executed by a simulated annealing-based algorithm with a time-dependent cooling schedule. The neighbourhood relation is determined by the pull-move set. The results provide experimental evidence that the maximum depth D of local minima of the underlying energy landscape can be upper bounded by D<n2/3. The local search procedure employs the stopping criterion (m/δ)D/γ, where m is an estimation of the average number of neighbouring conformations, γ relates to the mean of non-zero differences of the objective function for neighbouring conformations, and 1−δ is the confidence that a minimum conformation has been found. The bound complies with the results obtained for the ten benchmark problems.en
dc.language.isoeng
dc.relation.ispartofComputational Biology and Chemistry
dc.subjectprotein folding
dc.subjectHP-model
dc.subjectlandscape analysis
dc.subjectstochastic local search
dc.subjectsimulated annealing
dc.titleStochastic protein folding simulation in the three-dimensional HP-modelen
dc.contributor.institutionSchool of Computer Science
dc.contributor.institutionScience & Technology Research Institute
dc.description.statusPeer reviewed
rioxxterms.versionofrecordhttps://doi.org/10.1016/j.compbiolchem.2008.03.004
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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