title: Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference.
abstract: Functionally relevant conformational states of intrinsically disordered proteins (IDPs) are typically concealed in a vast space of fast interconverting structures. Here we present a novel methodology, NMR-based paramagnetic relaxation interference (PRI), that allows for direct observation of concerted motions and cooperatively folded sub-states in IDPs. The proposed NMR technique is based on the exploitation of cross correlated electron-nuclear dipolar relaxation interferences in doubly spin-labeled proteins and probes the transient spatial encounter of electron-nucleus spin pairs.
authors.affiliation: Department for Structural and Computational Biology Max F. Perutz Laboratories, University of Vienna Vienna Biocenter Campus 5, 1030 Vienna, Austria. Robert.Konrat@univie.ac.at.
authors.forename: D
authors.initials: D
authors.lastname: Kurzbach
authors.affiliation: Department for Structural and Computational Biology Max F. Perutz Laboratories, University of Vienna Vienna Biocenter Campus 5, 1030 Vienna, Austria. Robert.Konrat@univie.ac.at.
authors.forename: A
authors.initials: A
authors.lastname: Vanas
authors.affiliation: Department for Structural and Computational Biology Max F. Perutz Laboratories, University of Vienna Vienna Biocenter Campus 5, 1030 Vienna, Austria. Robert.Konrat@univie.ac.at.
authors.forename: A G
authors.initials: AG
authors.lastname: Flamm
authors.affiliation: Department for Structural and Computational Biology Max F. Perutz Laboratories, University of Vienna Vienna Biocenter Campus 5, 1030 Vienna, Austria. Robert.Konrat@univie.ac.at.
authors.forename: N
authors.initials: N
authors.lastname: Tarnoczi
authors.affiliation: Department for Structural and Computational Biology Max F. Perutz Laboratories, University of Vienna Vienna Biocenter Campus 5, 1030 Vienna, Austria. Robert.Konrat@univie.ac.at.
authors.forename: G
authors.initials: G
authors.lastname: Kontaxis
authors.affiliation: Institute for Physical Chemistry Martin-Luther-Universität Halle-Wittenberg von-Danckelmann-Platz 4, 06120 Halle (Saale), Germany.
authors.forename: N
authors.initials: N
authors.lastname: Maltar-Strmečki
authors.affiliation: Institute for Physical Chemistry Martin-Luther-Universität Halle-Wittenberg von-Danckelmann-Platz 4, 06120 Halle (Saale), Germany.
authors.forename: K
authors.initials: K
authors.lastname: Widder
authors.affiliation: Institute for Physical Chemistry Martin-Luther-Universität Halle-Wittenberg von-Danckelmann-Platz 4, 06120 Halle (Saale), Germany.
authors.forename: D
authors.initials: D
authors.lastname: Hinderberger
authors.affiliation: Department for Structural and Computational Biology Max F. Perutz Laboratories, University of Vienna Vienna Biocenter Campus 5, 1030 Vienna, Austria. Robert.Konrat@univie.ac.at.
authors.forename: R
authors.initials: R
authors.lastname: Konrat
mesh_terms: D004578:Electron Spin Resonance Spectroscopy; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D064267:Intrinsically Disordered Proteins