Solid-state NMR triple-resonance backbone assignments in a protein.
Triple-resonance solid-state NMR spectroscopy is demonstrated to sequentially assign the 13C' and 15N amide backbone resonances of adjacent residues in an oriented protein sample. The observed 13C' chemical shift frequency provides an orientational constraint complementary to those measured from the 1H and 15N amide resonances in double-resonance experiments.
Tan
W M
WM
Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA.
Gu
Z
Z
Zeri
A C
AC
Opella
S J
SJ
D002213:Capsid / Q000737:chemistry*; D002247:Carbon Isotopes; D006859:Hydrogen; D017912:Inovirus; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen