title: Thermodynamics of partly folded intermediates in proteins.
abstract: 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 parameters for folding intermediates of alpha-lactalbumin, apomyoglobin, cytochrome c, and staphylococcal nuclease has provided new insights on the nature of the forces involved in the stabilization of nascent protein structures. In this review, I summarize those results and discuss the structural implications of the observed thermodynamic behavior.
authors.affiliation: Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA.
authors.forename: E
authors.initials: E
authors.lastname: Freire
mesh_terms: D000465:Algorithms; D002151:Calorimetry; D006358:Hot Temperature; D007768:Lactalbumin / Q000737:chemistry; D008836:Micrococcal Nuclease / Q000737:chemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D007768:Lactalbumin; D008836:Micrococcal Nuclease