STRUCTURAL AND CONFORMATIONAL STUDY OF PEPTIDES CONTAINING GLYCINE AND ALANINE RESIDUES BY C-13 CPMAS NMR-SPECTROSCOPY IN SOLID-STATE

The results of the structural and conformational studies carried out u sing C-13 CPMAS NMR technique on several glycine and alanine containin g peptides in the solid state are reported. The study demonstrates the effects of variations in C-13 chemical shifts due to conformation and hydrogen bonding. The possibility of applying this technique to obtai n insight into the conformational characteristics of peptides of unkno wn structures is discussed.