Unlike the 'first' genetic code, however, the protein folding code remains largely uncracked. Although the code is so complex that it is unlikely to be cracked by any one research effort, biologists, computer scientists, and chemists are chipping away at it by different approaches. By these studies, researchers hope to gain an enhanced understanding of protein folding. This understanding has broad implications for the biomedical sciences and promises greater insight into the chemical basis for biology. Among the many benefits of this research would be an improved ability to predict the structures and functions of proteins discovered by the Human Genome Project, and to design new drugs rationally to interact with these proteins.
Chemists often study problems by constructing models.
By building compounds that resemble folded proteins, we are beginning to discover more about the factors that affect protein structure and stability. In these model systems, molecular templates induce b -sheet structure in adjacent peptide strands. The tert-butyl groups were necessary to render this tricyclic molecular template sufficiently soluble in organic solvents. I and other members of the Rebek group used this template as a building block for molecular receptors and self-replicating molecules. To make matters worse, the pentacyclic intermediates were not very soluble in organic solvents.