Open AccessThe assignment of the 1 H nuclear magnetic resonance spectrum of azurin
Author(s) -
CANTERS Gerard W.,
HILL H. Allen O.,
KITCHEN Nicholas A.,
ADMAN Elinor T.
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb07893.x
Subject(s) - azurin , histidine , chemistry , tyrosine , copper protein , tryptophan , copper , phenylalanine , resonance (particle physics) , metalloprotein , residue (chemistry) , nuclear magnetic resonance , crystallography , stereochemistry , amino acid , biochemistry , organic chemistry , physics , enzyme , atomic physics
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.