EPR distance measurements in deuterated proteins

J Magn Reson. 2010 Nov;207(1):164-7. doi: 10.1016/j.jmr.2010.08.002. Epub 2010 Aug 11.


One of the major problems facing distance determination by pulsed EPR, on spin-labeled proteins, has been the short relaxation time T(m). Solvent deuteration has previously been used to slow relaxation and so extend the range of distance measurement and sensitivity. We demonstrate here that deuteration of the underlying protein, as well as the solvent, extends the T(m) to a considerable degree. Longer T(m) gives greatly enhanced sensitivity, much extended distance measurement, more reliable distance distribution calculation and better baseline correction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Bacteria / growth & development
  • Deuterium / chemistry
  • Electron Spin Resonance Spectroscopy
  • Histones / chemistry
  • Histones / isolation & purification
  • Isotope Labeling
  • Protein Folding
  • Proteins / chemistry*
  • Proteins / isolation & purification
  • Solvents
  • Spin Labels


  • Histones
  • Proteins
  • Solvents
  • Spin Labels
  • Deuterium