Thermodynamics of partly folded intermediates in proteins

Research output: Contribution to journalReview articlepeer-review

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 languageEnglish (US)
Pages (from-to)141-165
Number of pages25
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume24
DOIs
StatePublished - 1995

Keywords

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

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

Fingerprint Dive into the research topics of 'Thermodynamics of partly folded intermediates in proteins'. Together they form a unique fingerprint.

Cite this