ArticleJournal of chemical theory and computation2014
Quantifying the Sources of Kinetic Frustration in Folding Simulations of Small Proteins.
Article in Journal of chemical theory and computation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Deep clustering of protein folding simulations.BMC bioinformatics · 2018Article
- Approximating frustration scores in complex networks via perturbed Laplacian spectra.Physical review. E, Statistical, nonlinear, and soft matter physics · 2015Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Experiments and atomistic simulations of polypeptides have revealed structural intermediates that promote or inhibit conformational transitions to the native state during folding. We invoke a concept of "kinetic frustration" to quantify the prevalence and impact of these behaviors on folding rates within a large set of atomistic simulation data for 10 fast-folding proteins, where each protein's conformational space is represented as a Markov state model of conformational transitions. Our graph theoretic approach addresses what conformational features correlate with folding inhibition and therefore permits comparison among features within a single protein network and also more generally between proteins. Nonnative contacts and nonnative secondary structure formation can thus be quantitatively implicated in inhibiting folding for several of the tested peptides.
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Registered trials
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