The investigators are trying to identify unnatural polymeric backbones that adopt compact, specific and predictable conformations ("foldamers"). The inspiration for this work comes from biology: living systems overwhelmingly employ polymers (protein and RNA) to carry out complex chemical operations like catalysis and tight, specific binding. Proteins and RNA are unique relative to other known polymers, natural or synthetic, in that these biofoldamers fold to compact conformations; the folding process generates "active sites" via precise spatial arrangement of reactive moieties scattered along the backbone. Therefore, if the investigators can identify new foldamer backbones with properties and capabilities analogous to but distinct from those of the biofoldamers. These hypothetical entities could be useful in a variety of applications:, including as medicinal agents, where they would presumably benefit from resistance to enzymatic degradation. Foldamer research is also likely to provide new scaffolds for combinatorial drug development; such systems should be particularly well suited to antagonism of specific protein-protein recognition. Preliminary results demonstrate that relatively small beta-amino acids oligomers ("beta- peptides") can adopt very stable helical conformations in solution. They plan to use this secondary structural element to construct "beta- proteins" with helical bundle tertiary structures, and will also explore the stabilization of alternative secondary structures with other beta-amino acids.