Prediction the energetics of osmolyte-induced protein folding/unfolding

Matthew Auton, D. Wayne Bolen

Research output: Contribution to journalArticlepeer-review

333 Scopus citations


A primary thermodynamic goal in protein biochemistry is to attain predictive understanding of the detailed energetic changes that are responsible for folding/unfolding. Through use of recently determined free energies of side-chain and backbone transfer from water to osmolytes and Tanford's transfer model, we demonstrate that the long-sought goal of predicting solvent-dependent cooperative protein folding/unfolding free-energy changes (m values) can be achieved. Moreover, the approach permits dissection of the folding/unfolding free-energy changes into individual contributions from the peptide backbone and residue side chains.

Original languageEnglish (US)
Pages (from-to)15065-15068
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number42
StatePublished - Oct 18 2005


  • Group transfer free energies
  • Transfer model
  • m value

ASJC Scopus subject areas

  • General


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