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 α-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.
Original language | English (US) |
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Pages (from-to) | 141-165 |
Number of pages | 25 |
Journal | Annual Review of Biophysics and Biomolecular Structure |
Volume | 24 |
DOIs | |
State | Published - 1995 |
Keywords
- calorimetry
- folding intermediates
- molten globule
- protein folding
- thermodynamics
ASJC Scopus subject areas
- Biophysics
- Structural Biology