One-dimensional 1H-detected solid-state NMR experiment to determine amide-1H chemical shifts in peptides

A simple one-dimensional solid-state NMR experiment is proposed to detect amide proton chemical shifts directly in uniaxially oriented molecules under static experimental condition and powder samples under MAS. The efficacy of this method depends on the selective transfer of 15N transverse magnetization to 1H nuclei via the 1H–15N dipolar coupling and also on the procedure to acquire the 1H magnetization under 1H–1H dipolar decoupling. Experimental results obtained from an N-acetyl-l–15N-valyl-l–15N-leucine single crystal labeled with 15N at both the amide sites and a powder sample of [15N–Phe-16]-magainin2 are presented.