Data for: Conformational Dependence of Chemical Shifts in the Proline Rich Region of TAU Protein

Nuclear magnetic resonance (NMR) is an important method for structure elucidation of proteins, as it is an easy accessible and well understood method. To characterize intrinsically disordered proteins (IDPs) using computational models it is often necessary to analyze and integrate calculated observables with measurements derived from solution NMR experiments.

In this case study we investigate whether and which chemical shifts of the proline-rich region of Tau protein (residues 210-240) offer information about the conformational state to distinguish two different microscopic conformers. Using multiple computational methods, chemical shifts of those two conformationally distinct structures are calculated. The different methods are compared regarding their ability to compute chemical shifts that are sensitive to conformational change.

The analysis of the data shows significant differences between the available methods and gives suggestions to an improved pathway for ensemble reweighting. Nevertheless, the variation in the chemical shifts which are predicted for configurations that are commonly considered to belong to the same conformation is such that this obscures a comparison between distinct conformations. Conformational sensitivity is found for up to ∼26% of calculated chemical shifts. It is found to be unrelated with atom element and had minor relation with the change of the corresponding φ dihedral angle.