Heterogeneous dynamics in partially disordered proteins

Combination of novel isotopic labeling, NMR experiments and MD simulations reveal heterogeneous dynamics in partially disordered proteins.

Glutton: a tool for generating structural ensembles of partly disordered proteins from chemical shifts

Motivation 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. Results 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). Availability and implementation Glutton is freely available at https://github.com/YeeHo/Glutton. Supplementary information Supplementary data are available at Bioinformatics online.