Conformational dependence of chemical shifts in the proline rich region of TAU protein.

ABSTRACT: Nuclear magnetic resonance (NMR) is an important method for structure elucidation of proteins, as it is an easily 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, the chemical shifts of these two conformationally distinct structures are calculated. The different methods are compared regarding their ability to compute chemical s

SUBMITTER: Stockelmaier J 

PROVIDER: S-EPMC11373535 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature