Foldons as independently folding units of proteins

Anna R. Panchenko, Zaida Luthey-Schulten, Peter G. Wolynes

Research output: Contribution to journalArticlepeer-review


Independently folding units of proteins, foldons, have been identified by maxima in a scan of the ratio of an energetic stability gap to the energy variance of that segment's molten globule states, reflecting the requirement of minimal frustration. Foldon boundaries, unlike structural domains, depend on the sequence of the protein. Therefore, domains defined by purely structural criteria and the foldons of a given protein may differ in size and structure. The predicted foldons have been compared to the exons and structural modules. Statistical analysis indicates a strong correlation between the energetically determined foldons and Go's geometrically defined structural modules. There is only a weak correlation of foldons to exons.

Original languageEnglish (US)
Pages (from-to)312-315
Number of pages4
JournalPhysica D: Nonlinear Phenomena
Issue number2-4
StatePublished - Jan 1 1997


  • Configurational entropy
  • Exons
  • Folding domains
  • Protein folding
  • Structural domains

ASJC Scopus subject areas

  • Statistical and Nonlinear Physics
  • Mathematical Physics
  • Condensed Matter Physics
  • Applied Mathematics

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