Narrow 1H NMR linewidths can be obtained for fully protonated protein samples in the solid state by using ultrafast magic‐angle spinning (60 kHz). Medium‐size microcrystalline and noncrystalline proteins can be analyzed without any need for deuteration of the protein sample. This approach provides assignments of the backbone 1H, 15N, 13Cα, and 13CO resonances and yields information about 1H–1H proximities.

A magic angle spinning (MAS) NMR technique to transfer polarization from protons to a specific set of the (13)C spins is introduced for the study of biomolecular samples in the solid-state. Ultrafast (>60 kHz) MAS and low irradiation rf fields are used to achieve band-selective Hartmann-Hahn cross-polarization (CP) between the whole proton bath and carbons whose resonances are close to the (13)C-transmitter offset. When compared to conventional, broadband (1)H-(13)C CP, the band-selective experiment can be established without any loss of sensitivity when polarizing the aliphatic signals of a protein sample, and with a significant gain when polarizing carbonyls. This scheme can be used as a building block in 2D (13)C-(13)C homonuclear correlation experiments to obtain a faster and more sensitive characterization of biological solids.