Determining the mechanism by which the amino acid sequence of a protein directs the rapid and efficient folding of proteins to their native, functional forms remains one of the most challenging problems in molecular biophysics. The development of a folding code that specifies the three-dimensional structure adopted by a given sequence would complement the genetic code and complete the central dogma of molecular biology (DNA " RNA " Amino Acid Sequence" Functional Protein). Over the past decade, it has also become clear that failure to fold correctly and quickly can lead to numerous diseases. The goals of our lab are to obtain a molecular-level understanding of the folding mechanisms of several very common motifs and to use those insights to contribute to the development of a general theory of protein folding. More recently, we have become interested in applying these biophysical insights to the development of therapeutics for misfolding diseases.