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1k09
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(New page: 200px<br /><applet load="1k09" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k09" /> '''Solution structure of BetaCore, A Designed W...)
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Revision as of 16:37, 20 November 2007
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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 of sequences from [1] with NH2 as ligand. 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 Tue Nov 20 18:44:36 2007
