Shiftless nuclear magnetic resonance spectroscopy.
The acquisition and analysis of high resolution one- and two-dimensional solid-state nuclear magnetic resonance (NMR) spectra without chemical shift frequencies are described. Many variations of shiftless NMR spectroscopy are feasible. A two-dimensional experiment that correlates the dipole-dipole and dipole-dipole couplings in the model peptide , (15)N labeled N-acetyl-leucine is demonstrated. In addition to the resolution of resonances from individual sites in a single crystal sample, the bond lengths and angles are characterized by the two-dimensional powder pattern obtained from a polycrystalline sample.
Wu
Chin H
CH
Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0307, USA.
Opella
Stanley J
SJ
D002247:Carbon Isotopes / Q000737:chemistry; D007930:Leucine / Q000031:analogs & derivatives* / Q000737:chemistry; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D007930:Leucine; C088117:acetylleucine