Chemical shift correlation via RFDR: elimination of resonance offset effects.
It is shown that it is possible to effectively execute RFDR experiments with adiabatic inversion pulses and obtain resonance offset compensation that is superior to what can be achieved by conventional rectangular pulses. Employing 40-micros tanh/tan adiabatic pulses at a power level of approximately 38 kHz and a spinning speed of 12 kHz it is demonstrated that the range of resonance offset compensation achieved is sufficient to generate, via a single experiment, homonuclear chemical shift correlation spectra in the entire (13)C chemical shift range in peptides/proteins at the currently available field strengths.
Heise
Bert
B
Abteilung Molekulare Biophysik/NMR-Spektroskopie, Institut für Molekulare Biotechnologie, 07745 Jena, Germany.
Leppert
Jörg
J
Ohlenschläger
Oliver
O
Görlach
Matthias
M
Ramachandran
Ramadurai
R
D000596:Amino Acids / Q000737:chemistry; D002247:Carbon Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry; D013816:Thermodynamics
D000596:Amino Acids; D002247:Carbon Isotopes; D010455:Peptides; D011506:Proteins