X–1H rotational-echo double-resonance NMR for torsion angle determination of peptides

C–H and N–H rotational-echo double-resonance (REDOR) NMR is developed for determining torsion angles in peptides. The distance between an X spin such as 13C or 15N and a proton is measured by evolving the proton magnetization under REDOR-recoupled X–H dipolar interaction. The proton of interest is selected through its directly bonded heteronuclear spin Y. The sidechain torsion angle χ1 is extracted from a 13Cβ-detected Hβ–N distance, while the backbone torsion angle φ is extracted from an 15N-detected HN–C′ distance. The approach is demonstrated on three model peptides with known crystal structures to illustrate its utility.