Understanding the principles behind protein folding remains one of the greatest challenges in science. The protein folding problem has been studied for three decades, and despite the great progress in recent years, there are still many questions to be answered. Only with the synergy of experimentalists and theoreticians from diverse disciplines will this challenge be answered. Moreover, there are now new computational tools along with new experimental techniques being developed for the studies of in vivo and in vitro protein folding. It is very important to bring together these scientists who are pioneering these quantitative approaches to create a novel collaboration for answering the challenges in protein folding. This workshop in Tempe, Arizona, May 9-13, 2010, will bring together a select group of some of the world's leading scientists from physics, chemistry, mathematics, and engineering. All have unique expertise in various aspects of protein folding, experimentation, and computational modelling. Protein folding has advanced in recent years with the use of high performance computing. The workshop will address the dynamic and thermodynamic properties of protein folding and the role of flexibility in protein sequence-structure-function relationship. Simulation and theoretical methods will be discussed in application to protein stability, folding, specific pathways and enzymatic activity.
Proteins are among the most incredible molecular machines in living systems. Not only are they accurate, proficient and specific, but they also have the rare ability to acquire new functions and structures to carry out a diverse set of functions, from enzymes to cytoskeleton to membrane channels. When a protein folds into its unique 3-dimensional structure, it starts immediately performing its function that has been evolved through the years. Thus, protein folding is central in understanding of living things. The list of workshop participants represents a truly impressive and wide-ranging cast of established leaders in the field, plus some younger people who are starting to make an impact. The meeting is designed to consist of a set of highly focused and intimate sessions. Understanding protein folding and hence mis-folding, has implications for health and medicine. We will open the meeting to local attendees from Arizona State University and the University of Arizona, including graduate students and postdocs.
Proteins are building blocks of all living things. Long chains of molecules fold into globular clusters which has a simple function. Humans have over two thousand distinct proteins, each with its own individual folded structure and folding pathway. This workshop on Protein Folding Pathways was sponsored by the National Science Foundation and Arizona State University. This workshop discussed the properties of protein folding and flexibility. The combination of leading experts in theory and experiment promoted extensive discussion as to how to integrate the recent advances in theoretical techniques with experiment. Each talk was followed by extensive discussions. The workshop brought together mathematicians, computer scientists, physicists, chemists and biochemists to examine the basic issues involved which have proved illusive. Fundamental questions like how are proteins encoed to fold to the same global structure at a rapid speed were widely discussed. Folding proteins is somewhat akin to crumpling a piece of paper, although the analogy with origami where a definite final structure is reached along a prescribed pathway would probably be a better description. Progress in this area will lead to insights that can be used in genetic engineering and in the disease prevention and curing. The long discussions at the workshop synthesized useful routes for future progress.
