| Literature DB >> 27918140 |
Dennis Kurzbach1,2, Estel Canet1,2, Andrea G Flamm3, Aditya Jhajharia1,2, Emmanuelle M M Weber1,2, Robert Konrat3, Geoffrey Bodenhausen1,2.
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 in 1 H-15 N correlation spectra. Binding to the polysaccharide heparin was found to induce the unfolding of preformed structural elements in OPN.Entities:
Keywords: NMR spectroscopy; dynamic nuclear polarization; hyperpolarized water; intrinsically disordered proteins; solvent exchange
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Year: 2016 PMID: 27918140 DOI: 10.1002/anie.201608903
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336