title: Probing local backbone geometries in intrinsically disordered proteins by cross-correlated NMR relaxation.
abstract: An ultra-high-resolution NMR experiment for the measurement of intraresidue (1)H(i)-(15)N(i)-(13)C'(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.
authors.affiliation: Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw, Poland.
authors.forename: Jan
authors.initials: J
authors.lastname: Stanek
authors.forename: Saurabh
authors.initials: S
authors.lastname: Saxena
authors.forename: Leonhard
authors.initials: L
authors.lastname: Geist
authors.forename: Robert
authors.initials: R
authors.lastname: Konrat
authors.forename: Wiktor
authors.initials: W
authors.lastname: Koźmiński
mesh_terms: D003198:Computer Simulation; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins