STRUCTURE OF PEPTIDES AND POLYPEPTIDES IN THE SOLID-STATE AS ELUCIDATED BY NMR CHEMICAL-SHIFT

It is reviewed that through the observation of solid-state C-13 NMR ch emical shift, the main-chain conformation and hydrogen-bonded structur e of peptides, polypeptides and proteins in the solid state have been successfully elucidated, and the combination of solid stale C-13 NMR a nd chemical shift calculation by quantum chemistry is a powerful means for the structural characterization. Furthermore, it is briefly intro duced that solid state NMR of N-15 and O-17 nuclei is very useful for obtaining information about hydrogen-bonded structure. This review art icle is communicated on the basis of our recent works on structural ch aracterization of peptides and polypeptides including proteins in the solid state by high-resolution solid-state NMR spectroscopy and its co mbination with quantum chemical calculation. (C) 1998 Elsevier Science B.V.