Backbone dynamics and amide proton exchange at the two sides of the eremomycin dimer by 15N NMR

15 N-labelling of the glycopeptide antibiotic eremomycin has made possible the dynamic characterization of the two sides of the dimer; in the presence of acetate anion the backbone amides are dynamically equivalent and the fastest amide proton exchange rate was found at the heart of the binding pocket.