Various compounds were studied with solid-state 119Sn and 31P NMR spectroscopy and quantum chemical calculations. Connections were made between the shielding tensors and the geometric and electronic structures of the molecules. First, the 119Sn chemical shielding anisotropy of various para substituted tetraaryl tin compounds was shown to be dependent on the tilt angle of the phenyl rings. Tetrakis(o-tolyl) tin did not have the shielding anisotropy predicted by the tilt angle of the rings. It was suggested that ortho substitution distorts the structures of the phenyl rings causing the discrepancy. Analysis of the solid-state 31P NMR spectra of triphenylphosphorane ylides, Ph3P=CHC(O)R, determined that increasing the electron-donating effects of the R group decreased the δ33 component. Theoretical calculations showed that the component lay along the ylidic bond and was dependent on the difference in phosphorus-carbon bond lengths between the phenyl and ylidic bonds. Another study concerned the solid-state 31P NMR of the series of triphenylphosphine derivatives, PPh3-x(o-tolyl)x where x = 0 to 3. The addition of ortho methyl groups changed the position of the δ11 component which could be the result of the change in energy gap between the lone pair (HOMO) and σ* anti-bonding (LUMO). The solid-state 31P NMR spectra of deuterated piperazinium phosphonate and phosphonic acid were influenced by the shielding, dipolar and spin-spin interactions, as well as, second order quadrupolar effects. The spectrum of deuterated piperazinium phosphonate had a chemical shielding anisotropy of 130 ppm, an effective dipolar coupling of 2500 kHz and a one-bond phosphorus-deuterium J coupling of 90 Hz. The phosphorus-deuterium bond length was predicted to be 1.44(2) Å. A deuterium quadrupolar coupling constant of 104 kHz was obtained from the CP/MAS 2H spectrum. The non-axial symmetry of phosphonic acid complicated the analysis of the 31P spectrum. Phosphorus-deuterium bond lengths of 1.44(5) Å and 1.40(4) Å were obtained for the two inequivalent sites in the unit cell.