Solid state 13‐C NMR spectroscopy with special reference to proteins and their derivatives. A comparison with vibrational spectroscopic methods

Abstract

AbstractPossible applications of solid‐state NMR in studies on polypeptides and proteins are presented. Several examples of 13‐C CP/MAS NMR spectra are discussed in relation to model compounds and polypeptides from various sources. A comparison is made with vibrational spectroscopic methods. It is concluded that the CP/MAS NMR method is especially useful in elucidating secondary structures in the unperturbed state, and, thus, may also be useful in the study of various conditions involving the disturbance of biochemical equilibria (e.g. the skin disease psoriasis and β‐fibrilloses). In these cases the NMR method is more elucidative than vibrational spectroscopy. However, owing to the fact that multiple spectral scans must be performed, it is very time consuming. It therefore appears that high resolution Fourier transform infra‐red spectroscopy is a complementary method, but not as informative regarding structural details in secondary structures. Combining both methods together provides a powerful tool for structure analysis.