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The complete assignment of the aromatic proton nuclear magnetic resonances of the three tyrosine residues in hen lysozyme is reported. These assignments were made using double resonance techniques, specific chemical modifications of one residue (Tyr-23), and by interpretation of the effects of paramagnetic lanthanide ions. Some aspects of the behaviour of the tyrosine residues are reported, including pK values, reactivity towards modifying agents and conformational mobility.


Journal article


Eur J Biochem

Publication Date





99 - 103


4-Chloro-7-nitrobenzofurazan, Animals, Binding Sites, Chickens, Egg White, Gadolinium, Magnetic Resonance Spectroscopy, Muramidase, Protein Binding, Protein Conformation, Tyrosine