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Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water
Author(s) -
Kurzbach Dennis,
Canet Estel,
Flamm Andrea G.,
Jhajharia Aditya,
Weber Emmanuelle M. M.,
Konrat Robert,
Bodenhausen Geoffrey
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201608903
Subject(s) - intrinsically disordered proteins , chemistry , magnetization transfer , biophysics , magnetization , osteopontin , nuclear magnetic resonance , solvent , two dimensional nuclear magnetic resonance spectroscopy , biochemistry , stereochemistry , magnetic resonance imaging , physics , medicine , quantum mechanics , biology , magnetic field , radiology
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.