Molecular oxygen as a paramagnetic NMR probe of protein solvent exposure and topology

Authors

  • Irina Bezsonova,

    1. Department of Chemistry, University of Toronto, 80 St. George St. Toronto, ON, Canada M5S 1A8
    2. Program in Molecular Structure and Function, Hospital for Sick Children, 555 University Avenue, Toronto, ON, Canada M5G 1X8
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  • Julie Forman-Kay,

    1. Program in Molecular Structure and Function, Hospital for Sick Children, 555 University Avenue, Toronto, ON, Canada M5G 1X8
    2. Department of Biochemistry, University of Toronto, 1 King's College Circle, ON, Canada M5S 1A8
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  • R. Scott Prosser

    Corresponding author
    1. Department of Chemistry, University of Toronto, UTM, 3359 Mississauga Rd. North Mississauga, ON, Canada L5L 1C6
    • Department of Chemistry, University of Toronto, UTM, 3359 Mississauga Rd. North Mississauga, ON, Canada L5L 1C6
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Abstract

This review focuses on the applications of dissolved oxygen in NMR studies of protein topology. A brief discussion is given to explain the origin of O2-induced paramagnetic shifts and relaxation rate enhancements, which are seen for a variety of nuclei of biological interest—in particular 13C, 19F, and 1H. We also give examples of applications of paramagnetic effects from dissolved O2, which include studies of solvent exposure, hydrophobicity, transient contacts or local clustering in intrinsically disordered proteins, immersion depth in membranous systems, and topology of membrane proteins. © 2008 Wiley Periodicals, Inc. Concepts Magn Reson Part A 32A: 239–253, 2008.

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