ArticleBiophysical journal2002
Protein folding pathways and kinetics: molecular dynamics simulations of beta-strand motifs.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Quantifying the Sources of Kinetic Frustration in Folding Simulations of Small Proteins.Journal of chemical theory and computation · 2014Article
- Protein folding: then and now.Archives of biochemistry and biophysics · 2008Article
- Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet.Chemical reviews · 2006Review
- Self-assembly of the ionic peptide EAK16: the effect of charge distributions on self-assembly.Biophysical journal · 2004Article
- Thermodynamics and stability of a beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein models.Protein science : a publication of the Protein Society · 2004Article
- Assembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein models.Biophysical journal · 2004Article
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3 authors.
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Abstract
The folding pathways and the kinetic properties for three different types of off-lattice four-strand antiparallel beta-strand protein models interacting via a hybrid Go-type potential have been investigated using discontinuous molecular dynamics simulations. The kinetic study of protein folding was conducted by temperature quenching from a denatured or random coil state to a native state. The progress parameters used in the kinetic study include the squared radius of gyration R(2)(g), the fraction of native contacts within the protein as a whole Q, and between specific strands Q(ab). In the time series of folding, the denatured proteins undergo a conformational change toward the native state. The model proteins exhibit a variety of kinetic folding pathways that include a fast-track folding pathway without passing through an intermediate and multiple pathways with trapping into more than one intermediate. The kinetic folding behavior of the beta-strand proteins strongly depends on the native-state geometry of the model proteins and the size of the bias gap g, an artificial measure of a model protein's preference for its native state.
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