Intrinsic backbone preferences for protein folding are thought to be present in blocked amino acid oligomers. Experimentally determined structures of small peptides in solution are therefore of vital importance in understanding the assembly of proteins and the resulting primary, secondary and tertiary structures. This is a challenging task which typically requires several spectroscopic methods such as Raman, IR, NMR, UV-CD and VCD. In this proposal we would like to use D4 to measure directly the intra-molecular pair correlation functions to probe peptide structures stabilized with intra- and inter-molecular hydrogen bonds (C7, beta-turns). These results will be correlated, in particular, with conformation populations obtained from IR spectra. In particular, we wish to determine whether or not the C7 conformation exists in alanine oligomers in aqueous solution.