title: Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water.
abstract: Hyperpolarized water can selectively enhance NMR signals of rapidly exchanging protons in osteopontin (OPN), a metastasis-associated intrinsically disordered protein (IDP), at near-physiological pH and temperature. The transfer of magnetization from hyperpolarized water is limited to solvent-exposed residues and therefore selectively enhances signals in1H-15N correlation spectra. Binding to the polysaccharide heparin was found to induce the unfolding of preformed structural elements in OPN.
authors.affiliation: Departement de Chimie, Ecole Normale Supérieure, PSL Research University, UPMC Univ Paris 06, CNRS, Laboratoire des Biomolécules (LBM), 24 rue Lhomond, 75005, Paris, France.|Sorbonne Universites, UPMC Univ Paris 06, Ecole Normale Supérieure, CNRS, Laboratoire des Biomolécules (LBM), Paris, France.
authors.forename: Dennis
authors.initials: D
authors.lastname: Kurzbach
authors.affiliation: Departement de Chimie, Ecole Normale Supérieure, PSL Research University, UPMC Univ Paris 06, CNRS, Laboratoire des Biomolécules (LBM), 24 rue Lhomond, 75005, Paris, France.|Sorbonne Universites, UPMC Univ Paris 06, Ecole Normale Supérieure, CNRS, Laboratoire des Biomolécules (LBM), Paris, France.
authors.forename: Estel
authors.initials: E
authors.lastname: Canet
authors.affiliation: Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna BioCenter Campus 5, 1030, Vienna, Austria.
authors.forename: Andrea G
authors.initials: AG
authors.lastname: Flamm
authors.affiliation: Departement de Chimie, Ecole Normale Supérieure, PSL Research University, UPMC Univ Paris 06, CNRS, Laboratoire des Biomolécules (LBM), 24 rue Lhomond, 75005, Paris, France.|Sorbonne Universites, UPMC Univ Paris 06, Ecole Normale Supérieure, CNRS, Laboratoire des Biomolécules (LBM), Paris, France.
authors.forename: Aditya
authors.initials: A
authors.lastname: Jhajharia
authors.affiliation: Departement de Chimie, Ecole Normale Supérieure, PSL Research University, UPMC Univ Paris 06, CNRS, Laboratoire des Biomolécules (LBM), 24 rue Lhomond, 75005, Paris, France.|Sorbonne Universites, UPMC Univ Paris 06, Ecole Normale Supérieure, CNRS, Laboratoire des Biomolécules (LBM), Paris, France.
authors.forename: Emmanuelle M M
authors.initials: EM
authors.lastname: Weber
authors.affiliation: Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna BioCenter Campus 5, 1030, Vienna, Austria.
authors.forename: Robert
authors.initials: R
authors.lastname: Konrat
authors.affiliation: Departement de Chimie, Ecole Normale Supérieure, PSL Research University, UPMC Univ Paris 06, CNRS, Laboratoire des Biomolécules (LBM), 24 rue Lhomond, 75005, Paris, France.|Sorbonne Universites, UPMC Univ Paris 06, Ecole Normale Supérieure, CNRS, Laboratoire des Biomolécules (LBM), Paris, France.
authors.forename: Geoffrey
authors.initials: G
authors.lastname: Bodenhausen
mesh_terms: D006863:Hydrogen-Ion Concentration; D019906:Nuclear Magnetic Resonance, Biomolecular; D053495:Osteopontin / Q000737:chemistry*; D011134:Polysaccharides / Q000737:chemistry*; D011522:Protons; D012997:Solvents / Q000737:chemistry; D013696:Temperature; D014867:Water / Q000737:chemistry*
chemical_list: D011134:Polysaccharides; D011522:Protons; D012997:Solvents; D014867:Water; D053495:Osteopontin
keywords: NMR spectroscopy; dynamic nuclear polarization; hyperpolarized water; intrinsically disordered proteins; solvent exchange