Protein Folding 2009

Dear Colleagues,

In recent years protein folding often seems to have become synonymous with protein structure prediction. The field of protein folding is in fact considerably more encompassing than the ability to stitch together recurrent structural motifs into models that come closer to a target than those of competitors. The targets are moving, and as predictions become more sophisticated with each passing tournament, so does our appreciation of the intricacies of protein structure, function, and dynamics.

The papers in this issue highlight work at the frontiers of protein folding research. Topics include the behaviors of proteins under extreme or non-physiological environments such as the interactions of proteins with surfaces, synthetic matrices, chaotropes and kosmotropes, and the sheltering environment of chaperones. The mechanisms by which protein misfolding leads to disease remains a challenging and medically important problem. New experimental approaches and new ways of thinking about protein folding are described. And finally, there are papers that continue to address the fundamental unresolved problem of how protein sequences encode for the three-dimensional structures of proteins.

In a climate that often emphasizes the "biology" bottom line, it is refreshing to see basic science flourishing and needed as much as ever in research that may not translate to a pharmaceutical pill but that has and will continue to reveal fundamental insights into the roles of molecular structures in health and disease. Yes, protein folding has been "solved" many times over but it keeps presenting interesting problems and opportunities that should continue to challenge the most ambitious investigators for years to come.

Dr. Andrei Alexandrescu
Guest Editor