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BetaCore, a designed water soluble four‐stranded antiparallel β‐sheet protein
Author(s) -
Carulla Natàlia,
Woodward Clare,
Barany George
Publication year - 2002
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.4440102
Subject(s) - antiparallel (mathematics) , heteronuclear molecule , beta sheet , chemistry , crystallography , amide , hydrogen bond , protein structure , chemical shift , nuclear magnetic resonance spectroscopy , stereochemistry , molecule , physics , biochemistry , organic chemistry , quantum mechanics , magnetic field
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.