A Simple One-Dimensional Solid-State NMR Method to Characterize the Nuclear Spin Interaction Tensors Associated with the Peptide Bond

We propose a simple one-dimensional RF pulse sequence for the study of chemical shift and heteronuclear dipolar coupling tensors of oriented as well as unoriented solids. An off-resonance RF decoupling of protons during the signal acquisition of less sensitive nuclei is used to suppress homonuclear ¹ H- ¹ H dipolar interactions. This method is experimentally demonstrated on peptide samples selectively labeled with ¹⁵ N isotope.