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• W2892047176 abstract "Many proteins are partially disordered in physiological conditions and only fold, fully or partially, upon binding. Their structural analysis is challenging because the accessible information, typically chemical shifts (CS) from nuclear magnetic resonance experiments, are averages over broad ensembles of conformations. We aim to develop a database for the analysis of such data in terms of conformational distributions of the protein backbone rather than of individual high-resolution structures.Glutton is the largest available database linking CS and protein 3D structures (5270 entries organized in three levels) and is searchable via a python script. It generates statistical distributions of ϕ-ψ dihedral angles based on CS or vice versa. Such ϕ-ψ distributions are used to calculate structural ensembles of partially disordered proteins from their CS. For folded proteins, such ensembles are excellent starting points for further refinement with additional experimental restraints (structure determination) or computational methods (structure prediction).Glutton is freely available at https://github.com/YeeHo/Glutton.Supplementary data are available at Bioinformatics online." @default.
• W2892047176 created "2018-09-27" @default.
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• W2892047176 date "2018-09-04" @default.
• W2892047176 modified "2023-10-16" @default.
• W2892047176 title "Glutton: a tool for generating structural ensembles of partly disordered proteins from chemical shifts" @default.
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• W2892047176 doi "https://doi.org/10.1093/bioinformatics/bty755" @default.
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