1H-13C separated local field spectroscopy of uniformly 13C labeled peptides and proteins

J Magn Reson. 2010 Sep;206(1):105-11. doi: 10.1016/j.jmr.2010.06.011. Epub 2010 Jul 1.

Abstract

By incorporating homonuclear decoupling on both the (1)H and (13)C channels it is feasible to obtain high-resolution two-dimensional separated local field spectra of peptides and proteins that are 100% labeled with (13)C. Dual-PISEMO (Polarization Inversion Spin Exchange Modulated Observation) can be performed as a conventional two-dimensional experiment, or with windowed detection as a one-dimensional experiment that offers flexibility as a building block for shiftless and other multidimensional triple-resonance experiments with the inclusion of (15)N irradiation. The triple-resonance MAGC probe used to perform these experiments at 500 MHz is described.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Bacteriophages / chemistry
  • Carbon Radioisotopes / chemistry*
  • Electromagnetic Fields
  • Hydrogen / chemistry*
  • Indicators and Reagents
  • Isotope Labeling / methods*
  • Magnetic Resonance Spectroscopy / instrumentation
  • Magnetic Resonance Spectroscopy / methods*
  • Nitrogen Isotopes
  • Peptides / analysis*
  • Proteins / analysis*
  • Spin Labels

Substances

  • Carbon Radioisotopes
  • Indicators and Reagents
  • Nitrogen Isotopes
  • Peptides
  • Proteins
  • Spin Labels
  • Hydrogen