Thermodynamics of partly folded intermediates in proteins

Ernesto Freire

Research output: Contribution to journalReview articlepeer-review

100 Scopus citations


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 languageEnglish (US)
Pages (from-to)141-165
Number of pages25
JournalAnnual Review of Biophysics and Biomolecular Structure
StatePublished - 1995


  • calorimetry
  • folding intermediates
  • molten globule
  • protein folding
  • thermodynamics

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology


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