The amide proton NMR chemical shift and hydrogen-bonded structure of peptides and polypeptides in the solid state as studied by high-frequency solid-state 1H NMR

High-resolution H-1 NMR spectra of glycine (Gly)-containing peptides and polypeptides in the solid state were measured at 800 MHz and at high-speed magic-angle spinning (MAS) of 30 kHz to elucidate the relationship between the hydrogen-bond length and H-1 NMR chemical shift to add to our previous experimental and theoretical findings that there is a relationship between the hydrogen-bond length and C-13, N-15 and O-17 chemical shifts of various kinds of amino acid residues of peptides and polypeptides in the solid state. From these experimental results, it is found that the H-1 chemical shifts of Gly amide protons of Gly-containing peptides and polypeptides, for which the hydrogen-bond length between the nitrogen and oxygen atoms (R-N ... O) have already been determined by X-ray diffraction, move downfield with a decrease in R-N ... O. Theoretical calculations qualitatively explain these experimental results. (C) 2000 Published by Elsevier Science B.V.