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

摘要

High-resolution ~1H NMR spectra of glycine (Gly)-containing peptides and polypeptides in the solid state were measured at 800 MHz and at high-speed magic-angle-spining (MAS) of 30 kHz to elucidate the relationship between the hydrogen-bond length and ~1H NMR chemical shift to add to our previous experimental and theoretical findings that there is a relationship between the hydrogen-bond length and ~(13)C,~(15)N and ~(17)O 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 ~1H chemical shifts of Gly amide protons of Gly-containing peptides and polypeptides, for which the hydrogen-bond length between the nitogen and oxygen atoms (R_(N centre dot centre dot centre dot O)have already been determined by X-ray diffraction,move downfield with a decrease in R_(centre dot centre dot centre dot O).Theoretical calculations qualitatively explain these experimental results.