SSNMR methods for determining structure in nucleosides and peptide

Structure determination in biologically relevant compounds is the theme linking this thesis together. The necessary theory to determine structure in the solid state using NMR is described. Additionally software (V r) was written and is described which may be used to simulate solid state NMR spectra under a variety of conditions. Experimental methods to determine chemical shift anisotropy tensors and their orientations are discussed as well as the homonuclear dipolar recoupling sequence DRAWS and its experimetal implementation. Two applications of structure determination in biological compounds are performed. First, the 15N chemical shift anisotropy tensor values and orientations in the prymidine nucleosides are determined in the solid state. Secondly, DRAWS based methods for determining the backbone ( f,y ) torsion angles of peptides and proteins in the solid state are discussed. In particular two experiments to measure the distance between adjacent carbonyl carbons in peptides are characterized as well as an experiment which measures the relative orientation between the two adjacent carbonyl carbons.