1k09 | pdb_00001k09
Solution structure of BetaCore, A Designed Water Soluble Four-Stranded Antiparallel b-sheet Protein
Overview
BetaCore is a designed approximately 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 beta-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 beta-sheet that folds in water.
About this Structure
1K09 is a Protein complex structure. Full crystallographic information is available from OCA.
Reference
BetaCore, a designed water soluble four-stranded antiparallel beta-sheet protein., Carulla N, Woodward C, Barany G, Protein Sci. 2002 Jun;11(6):1539-51. PMID:12021452 Page seeded by OCA on Fri May 2 22:08:25 2008
