Homonuclear decoupled 13C chemical shift anisotropy in 13C doubly labeled peptides by selective-pulse solid-state NMR.
We describe a new experiment for measuring homonuclear-decoupled anisotropic chemical shift patterns in doubly 13C-labeled compounds under magic-angle spinning. The experiment combines a pair of selective and non-selective 180 degrees pulses to suppress the 13C-13C scalar and dipolar interactions. This is combined with the recently developed SUPER technique to recouple the chemical shift anisotropy. Demonstrations on 13Calpha and 13CO-labeled amino acids and peptides show that accurate chemical shift powder patterns can be obtained. This permits the use of chemical shift anisotropy for conformational studies of suitably extensively 13C-labeled peptides and proteins.
Hong
Mei
M
Department of Chemistry, Iowa State University, Ames, IA 50011, USA. mhong@iastate.edu
Yao
Xiaolan
X
D016880:Anisotropy; D002247:Carbon Isotopes / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*
D002247:Carbon Isotopes; D010455:Peptides