Abstract
It is reviewed that through the observation of solid-state 13C NMR chemical shift, the main-chain conformation and hydrogen-bonded structure of peptides, polypeptides and proteins in the solid state have been successfully elucidated, and the combination of solid state 13C NMR and chemical shift calculation by quantum chemistry is a powerful means for the structural characterization. Furthermore, it is briefly introduced that solid state NMR of 15N and 17O nuclei is very useful for obtaining information about hydrogen-bonded structure. This review article is communicated on the basis of our recent works on structural characterization of peptides and polypeptides including proteins in the solid state by high-resolution solid-state NMR spectroscopy and its combination with quantum chemical calculation.
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