A luminescence method for determining the state of aromatic amino acids (tyrosine and tryptophan) in proteins and enzyme systems

Data on the relationship between the luminescent properties of aromatic amino acid residues and their physico-chemical properties in the protein macromolecule are presented. Some techniques and procedures for studying such states in proteins are discussed. Findings are cited concerning changes in the state of tryptophan protein residues produced during enzymatic reactions of urease and myosin.