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dc.contributor.authorVieth, Michal
dc.contributor.authorKolinski, Andrzej
dc.contributor.authorBrooks, C. L., III
dc.contributor.authorSkolnick, Jeffrey
dc.date.accessioned2009-05-14T14:20:06Z
dc.date.available2009-05-14T14:20:06Z
dc.date.issued1996
dc.identifier.citationDIMACS Series in Discrete Mathematics and Theoretical Computer Science, 23 (1996) 233-236en
dc.identifier.issn1052-1798
dc.identifier.urihttp://hdl.handle.net/1853/27922
dc.descriptionFirst published in DIMACS Series in Discrete Mathematics and Theoretical Computer Science, 23 (1996) published by the American Mathematical Society.en
dc.descriptionPresented at DIMACS Workshop on Global Minimization of Nonconvex Energy Functions: Molecular Conformation and Protein Folding, March 20-21, 1995.
dc.description.abstractA hierarchical approach to protein folding is employed to examine the folding pathway and predict the quaternary structure of the GCN4 leucine zipper. Structures comparable in quality to experiment have been predicted. In addition, the equilibrium between dimers, trimers and tetramers of a number of GCN4 mutants has been examined. In five out of eight cases, the simulation results are in accordance with the experimental studies of Harbury, et al.en
dc.language.isoen_USen
dc.publisherGeorgia Institute of Technologyen
dc.subjectProtein foldingen
dc.subjectGCN4 leucine zipperen
dc.subjectComputer simulationsen
dc.subjectLattice protein modelsen
dc.titleA hierarchical approach to the prediction of the quaternary structure of GCN4 and its mutantsen
dc.typeProceedingsen
dc.contributor.corporatenameScripps Research Institute
dc.publisher.originalAmerican Mathematical Society


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