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Keywords:

  • solution NMR;
  • topology;
  • solvent exposure;
  • membrane proteins;
  • immersion depth;
  • oxygen;
  • paramagnetic effects

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.