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Zheng, W., Andrec, M., Gallicchio, E., Levy, R. M. (2007) Simulating replica exchange simulations of protein folding with a kinetic network model. Proceedings of the National Academy of Sciences, 104 (39) 15340-15345 doi:10.1073/pnas.0704418104

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Reference TypeJournal (article/letter/editorial)
TitleSimulating replica exchange simulations of protein folding with a kinetic network model
JournalProceedings of the National Academy of Sciences
AuthorsZheng, W.Author
Andrec, M.Author
Gallicchio, E.Author
Levy, R. M.Author
Year2007 (September 25)Volume104
Issue39
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0704418104Search in ResearchGate
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Mindat Ref. ID1742712Long-form Identifiermindat:1:5:1742712:0
GUID0
Full ReferenceZheng, W., Andrec, M., Gallicchio, E., Levy, R. M. (2007) Simulating replica exchange simulations of protein folding with a kinetic network model. Proceedings of the National Academy of Sciences, 104 (39) 15340-15345 doi:10.1073/pnas.0704418104
Plain TextZheng, W., Andrec, M., Gallicchio, E., Levy, R. M. (2007) Simulating replica exchange simulations of protein folding with a kinetic network model. Proceedings of the National Academy of Sciences, 104 (39) 15340-15345 doi:10.1073/pnas.0704418104
In(2007, September) Proceedings of the National Academy of Sciences Vol. 104 (39) Proceedings of the National Academy of Sciences

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Andrec, M., Felts, A. K., Gallicchio, E., Levy, R. M. (2005) Protein folding pathways from replica exchange simulations and a kinetic network model. Proceedings of the National Academy of Sciences, 102 (19) 6801-6806 doi:10.1073/pnas.0408970102
Zheng, Weihua, Andrec, Michael, Gallicchio, Emilio, Levy, Ronald M. (2009) Recovering Kinetics from a Simplified Protein Folding Model Using Replica Exchange Simulations: A Kinetic Network and Effective Stochastic Dynamics. The Journal of Physical Chemistry B, 113 (34). 11702-11709 doi:10.1021/jp900445t
Zheng, Weihua, Andrec, Michael, Gallicchio, Emilio, Levy, Ronald M. (2008) Simple Continuous and Discrete Models for Simulating Replica Exchange Simulations of Protein Folding†. The Journal of Physical Chemistry B, 112 (19). 6083-6093 doi:10.1021/jp076377+
Zheng, Weihua, Gallicchio, Emilio, Deng, Nanjie, Andrec, Michael, Levy, Ronald M. (2011) Kinetic Network Study of the Diversity and Temperature Dependence of Trp-Cage Folding Pathways: Combining Transition Path Theory with Stochastic Simulations. The Journal of Physical Chemistry B, 115 (6). 1512-1523 doi:10.1021/jp1089596
Pitera, J. W., Swope, W. (2003) Understanding folding and design: Replica-exchange simulations of ``Trp-cage'' miniproteins. Proceedings of the National Academy of Sciences, 100 (13) 7587-7592 doi:10.1073/pnas.1330954100
Reshetnyak, Yana K., Andreev, Oleg A., Segala, Michael, Markin, Vladislav S., Engelman, Donald M. (2008) Energetics of peptide (pHLIP) binding to and folding across a lipid bilayer membrane. Proceedings of the National Academy of Sciences, 105 (40) 15340-15345 doi:10.1073/pnas.0804746105
Henry, E. R., Best, R. B., Eaton, W. A. (2013) Comparing a simple theoretical model for protein folding with all-atom molecular dynamics simulations. Proceedings of the National Academy of Sciences, 110 (44) 17880-17885 doi:10.1073/pnas.1317105110
Schulman, R., Winfree, E. (2007) Synthesis of crystals with a programmable kinetic barrier to nucleation. Proceedings of the National Academy of Sciences, 104 (39) 15236-15241 doi:10.1073/pnas.0701467104
Kim, Y. C., Tang, C., Clore, G. M., Hummer, G. (2008) Replica exchange simulations of transient encounter complexes in protein-protein association. Proceedings of the National Academy of Sciences, 105 (35) 12855-12860 doi:10.1073/pnas.0802460105
Lowe, A. R., Itzhaki, L. S. (2007) Rational redesign of the folding pathway of a modular protein. Proceedings of the National Academy of Sciences, 104 (8) 2679-2684 doi:10.1073/pnas.0604653104
Cellmer, T., Buscaglia, M., Henry, E. R., Hofrichter, J., Eaton, W. A. (2011) Making connections between ultrafast protein folding kinetics and molecular dynamics simulations. Proceedings of the National Academy of Sciences, 108 (15) 6103-6108 doi:10.1073/pnas.1019552108
 
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