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Tryptophan fluorescence lifetimes in lysozyme.
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pH dependence of individual tryptophan N-1 hydrogen exchange rates in lysozyme and its chemically modified derivatives.
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Two-dimensional fluorescence correlation spectroscopy IV: resolution of fluorescence of tryptophan residues in alcohol dehydrogenase and lysozyme.
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Conformational studies on modified proteins and peptides. IV. Conformation of lysozyme derivatives modified at tyrosine or at tryptophan residues.
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10
The selective quenching of tryptophan fluorescence in proteins by iodide ion: lysozyme in the presence and absence of substrate.
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FLUORESCENCE AND THE STRUCTURE OF PROTEINS. II. FLUORESCENCE OF PEPTIDES CONTAINING TRYPTOPHAN OR TYROSINE.
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STRUCTURE OF MURAMIDASE (LYSOZYME). I. THE EFFECT OF GUANIDINE HYDROCHLORIDE ON MURAMIDASE.
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Fluorescence of lysozyme and lysozyme substrate complexes. Separation of tryptophan contributions by fluorescence difference methods.
J Biol Chem. 1967 Oct 25;242(20):4644-51.
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The fluorescence of lysozyme and lysozyme substrate complexes.
Biochem Biophys Res Commun. 1966 Apr 19;23(2):133-8. doi: 10.1016/0006-291x(66)90517-1.
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Structure of lysozyme. X. On the structural role of tryptophan residues.
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The position of the active tryptophan residue in lysozyme.
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Varying luminescence behavior of the different tryptophan residues of papain.
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Separation of contributions of tryptophans and tyrosines to the ultraviolet circular dichroism spectrum of hen egg-white lysozyme.
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Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. 3. Dependence on temperature.
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Intramolecular singlet excitation transfer. Applications to polypeptides.
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