The protein folding problem has long been regarded as a fundamental mystery blocking our understanding of how the genetic information locked in DNA is transformed into a dynamic living organism. In the last decades, however, a basic understanding of the folding process has been achieved. The keys to this progress include borrowing theoretical ideas about energy landscapes from condensed matter physics and physical chemistry, employing powerful computer simulation techniques and bringing to bear new experimental tools such as single molecule methods and ultrafast spectroscopy, as well as elaborating the classical kinetic techniques of biophysical chemistry while exploiting the capabilities of protein engineering. Thus many communities from physics, chemistry and biology have merged to form the discipline of protein folding dynamics. Many of the fundamental issues about how proteins fold remain under intense investigation. New frontiers include understanding the diversity and basic time scales of folding larger proteins building on what has been learned in small model systems. Also we can now enquire how folding behavior has evolved in natural history, using huge quantities of genomic data. Folding is now known to be an emergent property. Recognizing this, to test our understanding, the community is now also exploring whether folding can be instantiated in completely novel designed systems, so-called "foldamers". Folding is not just a preliminary step to biological function but is intimately involved in functional processes such as allosteric change and molecular recognition. Furthermore the evolution of these capabilities has shown its mark on protein folding dynamics, an area of great ferment bringing together a new group of biologists. The misfolding of some proteins seems central to the progress of many diseases such as Alzheimer's and here the new tools of the folding community are bringing new insights. Finally we now can ask whether the hard won paradigms of protein folding dynamics gleaned from studying small globular proteins can be applied to membrane protein folding in which other biological actors are implicated as chaperones. Also can folding concepts be applied to studying how the very largest structures in the cell are organized, such as chromosomes? Sessions covering both new developments in the basic areas as well as applications of folding dynamics to more complex biology are planned.