Data for: Evaluating the Impact of Phosphorylation on the Dynamics of the Tau Protein Proline-Rich Region

The proline rich region of the tubulin associated unit (TAU) protein is of substantial interest in understanding neurodegenerative diseases due to its interaction with bridging integrator 1 (BIN1). The associated gene BIN1 is substantially associated with the development of Alzheimer’s disease. Previous studies have underlined the importance of the conformation of the proline rich region of TAU and the effect of its phosphorylation. In this study we investigate the change in compactness between a four times phosphorylated TAU fragment (210-240) compared to the unphoshorylated apo form using computational means. We apply our Ensemble Reconstruction from Fragments (ERF) approach to create two unbiased conformational ensembles, from which a reweighted ensemble is derived that agrees with observables from nuclear magnetic resonance experiments. The resulting shift of the radius of gyration indicates a preference for more compact conformations for the apo form, while the restraints derived from the experimental data do not substantially influence the compactness of the phosphorylated peptide.