2H NMR spectra of 2 H-labeled amino acids, peptides, and polypeptides, as prepared in this work, were measured in the solid state over a wide range of temperatures. From spectral simulations based on the 2 H dynamic NMR theory, NMR parameters such as quadrupolar coupling constant (e 2 qQ/h) and electric field gradient asymmetric parameter (η) were determined, and the relationship between these NMR parameters and the hydrogen-bond length (R N . .. O ) was elucidated. From the observed 2 H NMR spectra of amide N 2 H deuteron of peptides and polypeptides in the solid state, it was found that the e 2 qQ/h values decrease with a decrease in R N . .. O . This shows that the hydrogen-bond length of peptides and polypeptides can be evaluated through the observation of the e 2 qQ/h value of the amide deuteron. Further, the observed 2 H NMR spectra of the N 2 H 3 deuterons of 2 H-labeled Gly and GlyGly in the solid state, as a function of temperature, were analyzed with spectral simulations. From this result, the rotational barrier around the C α -N 2 H 3 bond was determined. On the other hand, from the observation of 2 H NMR spectra of 2 H-labeled GlyGly.HNO 3 and GlyGly.H 2 O.HCl in the solid state, it was found that the rate of the C 3 v rotation around the C α -NH 3 of these compounds is several MHz above in the temperature range 215-340K, and is higher than that observed for 2 H-labeled GlyGly.