Dynamics and Thermodynamics of β-Hairpin Assembly: Insights from Various Simulation Techniques

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dc.contributor.author Kolinski, Andrzej
dc.contributor.author Ilkowski, Bartosz
dc.contributor.author Skolnick, Jeffrey
dc.date.accessioned 2011-10-31T19:45:13Z
dc.date.available 2011-10-31T19:45:13Z
dc.date.issued 1999-12
dc.identifier.citation Kolinski, 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.issn 0006-3495
dc.identifier.uri http://hdl.handle.net/1853/41943
dc.description © 1999 by the Biophysical Society en_US
dc.description.abstract Small 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.iso en_US en
dc.publisher Georgia Institute of Technology en
dc.subject Globular proteins en
dc.subject Peptides en
dc.subject Simulation en
dc.subject Monte Carlo method en
dc.subject Protein folding en
dc.title Dynamics and Thermodynamics of β-Hairpin Assembly: Insights from Various Simulation Techniques en
dc.type Article en
dc.contributor.corporatename Uniwersytet Warszawski. Wydział Chemii
dc.contributor.corporatename Scripps Research Institute. Dept. of Molecular Biology
dc.publisher.original Biophysical Society

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