Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation

Jan Stanek, Saurabh Saxena, Leonhard Geist, Robert Konrat, Wiktor Koźmiński

An ultra-high-resolution NMR experiment for the measurement of intraresidue ¹H(i)–¹⁵N(i)–¹³C'(i) dipolar–chemical shift anisotropy relaxation interference is employed to extract information about local backbone geometries in intrinsically disordered proteins. The study of tumor suppressor BASP1 revealed a population shift of β-turn geometries at low pH conditions and a compaction of the BASP1 structural ensemble.