Pressure provides new insights into protein folding, dynamics and structure

Hydrostatic pressure is a powerful tool for studying protein folding, and t he dynamics and structure of folding intermediates. Recently, pressure tech niques have opened two important fronts to aid our understanding of how pol ypeptides fold into highly structured conformations. The first advance is t he stabilization of folding intermediates, making it possible to characteri ze their structures and dynamics by different methodologies. Kinetic studie s under pressure constitute the second advance, promising detailed appraisa l and understanding of protein folding landscapes. The combination of these two approaches enables dissection of the roles of packing and cavities in folding, and in assembly of multimolecular structures such as protein-DNA c omplexes and viruses. The study of aggregates and amyloids, derived from pa rtially folded intermediates at the junction between productive and off-pat hway folding, have also been studied, promising better understanding of dis eases associated with protein misfolding.