The assignment of the 1 H nuclear magnetic resonance spectrum of azurin

Abstract

A detailed assignment of the 1 H nuclear magnetic resonance spectrum of azurin has been made. Resonances associated with the single tryptophan residue, all six phenylalanine residues, one of the two tyrosine residues and all four histidine residues, as well as most of the resonances from the ring‐current shifted methyl groups have been assigned. These assignments have been used to study the pH dependence of the structure of the protein and binding of analogues of redox‐active reagents to the protein.