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dc.contributor.authorKolinski, Andrzej
dc.contributor.authorIlkowski, Bartosz
dc.contributor.authorSkolnick, Jeffrey
dc.date.accessioned2011-10-31T19:45:13Z
dc.date.available2011-10-31T19:45:13Z
dc.date.issued1999-12
dc.identifier.citationKolinski, A, Ilkowski B, Skolnick J. 1999. Dynamics and thermodynamics of beta-hairpin assembly: insights from various simulation techniques. Biophysical journal. 77(6):2942-52.en
dc.identifier.issn0006-3495
dc.identifier.urihttp://hdl.handle.net/1853/41943
dc.description© 1999 by the Biophysical Societyen_US
dc.description.abstractSmall peptides that might have some features of globular proteins can provide important insights into the protein folding problem. Two simulation methods, Monte Carlo Dynamics (MCD), based on the Metropolis sampling scheme, and Entropy Sampling Monte Carlo (ESMC), were applied in a study of a high-resolution lattice model of the C-terminal fragment of the B1 domain of protein G. The results provide a detailed description of folding dynamics and thermodynamics and agree with recent experimental findings (Munoz et al., 1997. Nature. 390:196–197). In particular, it was found that the folding is cooperative and has features of an all-or-none transition. Hairpin assembly is usually initiated by turn formation; however, hydrophobic collapse, followed by the system rearrangement, was also observed. The denatured state exhibits a substantial amount of fluctuating helical conformations, despite the strong b-type secondary structure propensities encoded in the sequence.en
dc.language.isoen_USen
dc.publisherGeorgia Institute of Technologyen
dc.subjectGlobular proteinsen
dc.subjectPeptidesen
dc.subjectSimulationen
dc.subjectMonte Carlo methoden
dc.subjectProtein foldingen
dc.titleDynamics and Thermodynamics of β-Hairpin Assembly: Insights from Various Simulation Techniquesen
dc.typeArticleen
dc.contributor.corporatenameUniwersytet Warszawski. Wydział Chemii
dc.contributor.corporatenameScripps Research Institute. Dept. of Molecular Biology
dc.publisher.originalBiophysical Society


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