BetaCore, a designed water soluble four-stranded antiparallel β-sheet protein

Natàlia Carulla, Clare Woodward, George Barany

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


BetaCore is a designed ∼50-residue protein in which two BPTI-derived core modules, CM I and CM II, are connected by a 22-atom cross-link. At low temperature and pH 3, homo- and heteronuclear NMR data report a dominant folded ('f') conformation with well-dispersed chemical shifts, i, i+1 periodicity, numerous long-range NOEs, and slowed amide hydrogen isotope exchange patterns that is a four-stranded antiparallel β-sheet with nonsymmetrical and specific association of CM I and CM II. BetaCore 'f' conformations undergo reversible, global, moderately cooperative, non-two-state thermal transitions to an equilibrium ensemble of unfolded 'u' conformations. There is a significant energy barrier between 'f' and 'u' conformations. This is the first designed four-stranded antiparallel β-sheet that folds in water.

Original languageEnglish (US)
Pages (from-to)1539-1551
Number of pages13
JournalProtein Science
Issue number6
StatePublished - 2002


  • Core modules
  • Cross-link
  • Protein design
  • Protein folding
  • β-sheet protein

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