Thermodynamics of protein folding and molecular recognition

Ernesto Freire

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


The successful development of a structural parameterization of the energetics of protein folding has permitted the incorporation of the func ions that define the enthalpy, entropy and heat capacity changes (i.e. the individual components of the Gibbs energy) into a statistical thermodynamic formalism that describes the equilibrium folding pathway of a protein. The general approach is to construct with the computer a large ensemble of conformational states, and then derive the most probable population distribution; i.e. the distribution of states that best accounts for a wide array of experimental observables. The accuracy of the approach is evaluated by comparison of predicted and experimental physical observables. This formalism has allowed the development of a computer program (Virtual Differential Scanning Calorimetry, VDSC) that generates the expected heat capacity function from a PDB data file containing the atomic coordinates of a protein; and a second program (CoreFHT) that predicts the NMR derived hydrogen exchange protection factors for individual amino acids.

Original languageEnglish (US)
Pages (from-to)2253-2261
Number of pages9
JournalPure and Applied Chemistry
Issue number11
StatePublished - Nov 1997

ASJC Scopus subject areas

  • General Chemistry
  • General Chemical Engineering


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