1H-13C separated local field spectroscopy of uniformly 13C labeled peptides and proteins.
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.
Lin
Eugene C
EC
Department of Chemistry and Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0307, USA.
Wu
Chin H
CH
Yang
Yuan
Y
Grant
Christopher V
CV
Opella
Stanley J
SJ
D001435:Bacteriophages / Q000737:chemistry; D002250:Carbon Radioisotopes / Q000737:chemistry*; D004574:Electromagnetic Fields; D006859:Hydrogen / Q000737:chemistry*; D007202:Indicators and Reagents; D007553:Isotope Labeling / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy / Q000295:instrumentation / Q000379:methods*; D009587:Nitrogen Isotopes; D010455:Peptides / Q000032:analysis*; D011506:Proteins / Q000032:analysis*; D013113:Spin Labels
D002250:Carbon Radioisotopes; D007202:Indicators and Reagents; D009587:Nitrogen Isotopes; D010455:Peptides; D011506:Proteins; D013113:Spin Labels; D006859:Hydrogen