The relationship between the amide proton chemical shift and the conformation of homopolypeptides in the solid state was studied using the H-1 combined rotation and multiple pulse spectroscopy (CRAMPS) NMR method. The main-chain amide proton signals are considerably broad due to the residual dipolar couplings between the quadrupolar N-14 nucleus and amide proton relative to other proton signals of solid polypeptides. We have prepared fully N-15-labeled (99 at. %) poly(L-alanines) ([Ala*](n)) and poly(L-leucines) ([Leu*](n)), adopting an alpha-helix or beta-sheet form to eliminate the effect of the quadrupolar N-14 nuclei, and then measured their H-1 CRAMPS NMR spectra by increasing the magic-angle spinning speed. Thus, the (NH)-N-15 proton chemical shifts of [Ala*](n) and [Leu*](n) were successfully determined to be 8.0-8.1 ppm (alpha-helix) and 8.6-9.1 ppm (beta-sheet). Accordingly, it became apparent that the amide proton chemical shifts are sensitive to the conformation of solid polypeptides.