Protons (¹H) are useful reporters of protein structure and dynamics in solid-state NMR. However, ¹H abundance is detrimental to the resolution of NMR spectra. Substituting ¹H by deuterons has been an efficient strategy to improve spectral quality, but when the crucial backbone amide sites are not protonated, much information is loss. We propose a method to completely protonate the amide sites, while maintaining high-resolution information, which partially also extends to backbone alpha-¹H.