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 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.
Freire
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Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA.
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
D007768:Lactalbumin; D008836:Micrococcal Nuclease