Show simple item record

dc.contributor.authorSikorski, Andrzej
dc.contributor.authorKolinski, Andrzej
dc.contributor.authorSkolnick, Jeffrey
dc.date.accessioned2011-10-31T19:45:13Z
dc.date.available2011-10-31T19:45:13Z
dc.date.issued1998-07
dc.identifier.citationSikorski, A, Kolinski A, Skolnick J. 1998. Computer simulations of de novo designed helical proteins. Biophysical journal. 75(1):92-105.en
dc.identifier.issn0006-3495
dc.identifier.urihttp://hdl.handle.net/1853/41942
dc.description© 1998 by the Biophysical Societyen_US
dc.description.abstractIn the context of reduced protein models, Monte Carlo simulations of three de novo designed helical proteins (four-member helical bundle) were performed. At low temperatures, for all proteins under consideration, protein-like folds having different topologies were obtained from random starting conformations. These simulations are consistent with experimental evidence indicating that these de novo designed proteins have the features of a molten globule state. The results of Monte Carlo simulations suggest that these molecules adopt four-helix bundle topologies. They also give insight into the possible mechanism of folding and association, which occurs in these simulations by on-site assembly of the helices. The low-temperature conformations of all three sequences have the features of a molten globule state.en
dc.language.isoen_USen
dc.publisherGeorgia Institute of Technologyen
dc.subjectGlobular proteinsen
dc.subjectMonte Carlo methoden
dc.subjectProtein foldingen
dc.subjectSimulationen
dc.titleComputer simulations of de novo designed helical proteinsen
dc.typeArticleen
dc.contributor.corporatenameUniwersytet Warszawski. Wydział Chemii
dc.contributor.corporatenameScripps Research Institute. Dept. of Molecular Biology
dc.publisher.originalBiophysical Society


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record