These intermolecular forces can include hydrogen bonding, hydrophobic forces, metal binding or electrostatic attractions. Specific areas of interest are receptor design, recognition of proteins and DNA, protein mimetics, and receptor-mediated chemical synthesis. Each type of secondary structure has a unique three-dimensional appearance. Alpha-helices twist back upon themselves to form a corkscrew shape. Beta-sheets contain several protein strands held in a linear extended conformation, with hydrogen bonds existing between adjacent strands.
Proteins are large molecules which can be difficult to synthesize.
Another way to study how proteins function is to create small molecules that mimic the shape and functionality of a protein, but can be easily synthesized in the laboratory. These peptidomimetics can help us understand the mechanisms of protein action and in some cases replace a large protein in a biological interaction. Peptidomimetics must position functionality in the right orientation, but must also maintain rigidity without the assistance of the entire globular protein. Our approach creates small molecules through organic synthesis which constrain peptide sidechains into the extended conformation of a beta-sheet. These templates rigidly hold the peptide strands in such as way as to promote the formation of hydrogen bonds between adjacent strands.