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Kim, S.-Y., Lee, J. and Lee, J. (2005) Folding Simulations of Small Proteins. Biophysical Chemistry, 115, 195-200. http://dx.doi.org/10.1016/j.bpc.2004.12.040

has been cited by the following article:

  • TITLE: Folding and Unfolding Simulations of a Three-Stranded Beta-Sheet Protein

    AUTHORS: Seung-Yeon Kim

    KEYWORDS: Protein, Folding, Unfolding, Computer Simulation

    JOURNAL NAME: Journal of Materials Science and Chemical Engineering, Vol.4 No.1, January 11, 2016

    ABSTRACT: Understanding the folding processes of a protein into its three-dimensional native structure only with its amino-acid sequence information is a long-standing challenge in modern science. Two- hundred independent folding simulations (starting from non-native conformations) and two- hundred independent unfolding simulations (starting from the folded native structure) are performed using the united-residue force field and Metropolis Monte Carlo algorithm for betanova (three-stranded antiparallel beta-sheet protein). From these extensive computer simulations, two representative folding pathways and two representative unfolding pathways are obtained in the reaction coordinates such as the fraction of native contacts, the radius of gyration, and the root- mean-square deviation. The folding pathways and the unfolding pathways are similar each other. The largest deviation between the folding pathways and the unfolding pathways results from the root-mean-square deviation near the folded native structure. In general, unfolding computer simulations could capture the essentials of folding simulations.