Rupley Ja scite author profile

In the first part of this Discussion the beautiful crystallographic results obtained at the Royal Institution were described (Blake, Mair et al ., p. 365, Blake, Johnson et al ., p. 378). Particular attention was paid to the nature of certain lysozymesaccharide complexes, some involving oligosaccharides of N -acetylglucosamine. This paper describes reactions of these same sugars, namely, their binding and cleavage by the enzyme.

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Comparison of protein structure in the crystal and in solution. III. Tritium-hydrogen exchange of lysozyme and a lysozyme-saccharide complex

Praissman¹,

Ja²

1968

Biochemistry

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Proton magnetic resonance study of the indole NH resonances of lysozyme. Assignment, deuterium exchange kinetics, and inhibitor binding

Jd¹,

Wd²,

Ja³

1971

J. Am. Chem. Soc.

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Rupley Ja

Insulin self-association. Spectrum changes and thermodynamics

Comparison of protein structure in the crystal and in solution. II. Tritium-hydrogen exchange of zinc-free and zinc insulin

The binding and cleavage by lysozyme of N -acetylglucosamine oligosaccharides

Comparison of protein structure in the crystal and in solution. III. Tritium-hydrogen exchange of lysozyme and a lysozyme-saccharide complex

Proton magnetic resonance study of the indole NH resonances of lysozyme. Assignment, deuterium exchange kinetics, and inhibitor binding

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