Organic Letters · 2006 · 55 citations · 19 references
Life SciencesBiochemistryChemistryOrganometallic ChemistryProtein-protein InteractionsStructural BiologyCoordination ChemistryDisulfide Bond FormationMetal-ligand BondingProtein ChemistryProtein ConformationProtein StructureDisulfide Bond ChemistryDisulfide Bond Formation In Protein InteractionsDisulfide Bond StructureDisulfide ContributionsMetal-binding ProteinsProtein Structure AlignmentResidual Dipolar Coupling AnalysisResidual Dipolar Couplings
[structure: see text] A short synthesis of EDTA-based metal chelates that can be attached to the cysteine residue of a protein via a disulfide bond is described. The complexes were used after coordination of lanthanides to align trigger factor and apo-calmodulin in solution to yield residual dipolar couplings and pseudocontact shifts. Alignment tensors for the new tags are linearly independent compared to those of previously published tags.
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