Recent advances in computer and software engineering have made it possible to monitor in real time and at atomistic resolution folding of some small proteins (e.g., FIP35, HP35). Does this mean that the gap between experiment and simulation is bridged for good? And that we can determine and experimentally validate free energy landscapes of proteins?

These are the central questions around which a number of leaders in protein folding will discuss and hopefully reach a consensus during the course of this workshop.

One open question is that of estimating the height of protein folding free energy barriers and, related, that of estimating a pre-exponential factor; current estimations of either vary broadly, depending on the experimental or computational techniques used and, crucially, on how data is analysed.

Can free energy landscapes be directly obtained from experiment alone? How? What are the assumptions, implicit or explicit, that one has to make? What are the possible sources of errors? These is currently a difference of opinions on these important issues. Can a consensus be reached?
The exactly same questions arise if one considers simulation instead of experiment, which are not simply answered by the possibility of unimaginably long simulation and unlimited time and space resolution.

The aim of this workshop is to bring theoretical, computational and experimental protein folding specialists together to thoroughly discuss a number of key issues, and in particular those on which there are currently different, if not opposite, opinions. We will consider this workshop a success if there will be agreement on some issues, and if agreement can be found on what it will take to solve issues that are still contentious.