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As a necessary first step in the use of heteronuclear correlated spectra to obtain high resolution solution structures of the protein, assignment of the 15 N NMR spectra of reduced and oxidized Escherichia coli thioredoxin (M r 12 000) uniformly labeled with 15 N has been performed. The 15 N chemical shifts of backbone amide nitrogen atoms have been determined...
Two-dimensional high resolution NMR techniques have been applied to study the structural differences between the oxidized and reduced forms of Escherichia coli thioredoxin in solution. Sequential proton resonance assignments indicate only limited conformational changes; major chemical shift differences are found for a few residues in a β-strand immediately preceding the active site S S bridge and...
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