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Coarse-Grained Modeling of the Interplay between Secondary Structure Propensities and Protein Fold Assembly

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cris.lastimport.scopus2024-02-12T20:17:48Z
dc.abstract.enWe recently developed a new coarse-grained model of protein structure and dynamics [Dawid et al. J. Chem. Theory Comput. 2017, 13(11), 5766−5779]. The model assumed a single bead representation of amino acid residues, where positions of such united residues were defined by centers of mass of four amino acid fragments. Replica exchange Monte Carlo sampling of the model chains provided good pictures of modeled structures and their dynamics. In its generic form the statistical knowledge-based force field of the model has been dedicated for single-domain globular proteins. Sequence-specific interactions are defined by three-letter secondary structure data. In the present work we demonstrate that different assignments and/or predictions of secondary structures are usually sufficient for enforcing cooperative formation of native-like folds of SURPASS chains for the majority of single-domain globular proteins. Simulations of native-like structure assembly for a representative set of globular proteins have shown that the accuracy of secondary structure data is usually not crucial for model performance, although some specific errors can strongly distort the obtained three-dimensional structures.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorDawid, Aleksandra E.
dc.contributor.authorGront, Dominik
dc.contributor.authorKoliński, Andrzej
dc.date.accessioned2024-01-24T19:30:46Z
dc.date.available2024-01-24T19:30:46Z
dc.date.copyright2018-02-27
dc.date.issued2018
dc.description.accesstimeAT_PUBLICATION
dc.description.financeNie dotyczy
dc.description.number4
dc.description.versionFINAL_PUBLISHED
dc.description.volume14
dc.identifier.doi10.1021/ACS.JCTC.7B01242
dc.identifier.issn1549-9618
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/103180
dc.languageeng
dc.pbn.affiliationchemical sciences
dc.relation.ispartofJournal of Chemical Theory and Computation
dc.relation.pages2277-2287
dc.rightsOther
dc.sciencecloudnosend
dc.titleCoarse-Grained Modeling of the Interplay between Secondary Structure Propensities and Protein Fold Assembly
dc.typeJournalArticle
dspace.entity.typePublication