Protein folding is undoubtedly one of the most challenging and important problems in biophysics. In the past four decades, extensive experimental and computational effort has been devoted to answering many questions such as: Why do proteins fold? How do proteins fold? How fast do proteins fold? What is the native structure of a given amino acid sequence? Tremendous progress has been made in all aspects of protein folding research, but the key questions are not fully answered. In recent years, principles learned from the study of soluble globular proteins are helping researchers understand intrinsically disordered proteins and “nonfolding events” such as aggregation, all of which have their unique biological roles in cellular function.

The purpose of this workshop is to assemble leading experts in the field to discuss lessons learned and to plan for the future. Of particular interest is to define what different approaches can be taken to address new questions. This seems to be particularly important for a field that has been around for a long time and is becoming increasingly active.