High-resolution solid-state H-2 NMR spectroscopy provides a method for measuring H-1 NMR chemical shifts in solids and is advantageous over the direct measurement of high-resolution solid-state H-1 NMR spectra, as it requires only the application of routine magic angle sample spinning (MAS) and routine H-1 decoupling methods, in contrast to the requirement for complex pulse sequences for homonuclear H-1 decoupling and ultrafast MAS in the case of high-resolution solid-state H-1 NMR. However, a significant obstacle to the routine application of high-resolution solid-state H-2 NMR is the very low natural abundance of H-2, with the consequent problem of inherently low sensitivity. Here, we explore the feasibility of measuring H-2 MAS NMR spectra of various solids with natural isotopic abundances at high magnetic field (850 MHz), focusing on samples of amino acids, peptides, collagen, and various organic solids. The results show that high-resolution solid-state H-2 NMR can be used successfully to measure isotropic H-1 chemical shifts in favorable cases, particularly for mobile functional groups, such as methyl and -N+H3 groups, and in some cases phenyl groups. Furthermore, we demonstrate that routine H-2 MAS NMR measurements can be exploited for assessing the relative dynamics of different functional groups in a molecule and for assessing whole-molecule motions in the solid state. The magnitude and field-dependence of second-order shifts due to the H-2 quadrupole interaction are also investigated, on the basis of analysis of simulated and experimental H-1 and H-2 MAS NMR spectra of fully deuterated and selectively deuterated samples of the alpha polymorph of glycine at two different magnetic field strengths.