THERMODYNAMICS OF PARTLY FOLDED INTERMEDIATES IN PROTEINS

Until recently, the energetics of protein-folding intermediates eluded direct measurement by high-sensitivity microcalorimetric techniques. But during the past year, the direct measurement of thermodynamic para meters for folding intermediates of alpha-lactalbumin, apomyoglobin, c ytochrome c, and staphylococcal nuclease has provided new insights on the nature of the forces involved in the stabilization of nascent prot ein structures. In this review, I summarize those results and discuss the structural implications of the observed thermodynamic behavior.