The binding and cleavage by lysozyme of N-acetylglucosamine oligosaccharides
@article{Rupley1967TheBA, title={The binding and cleavage by lysozyme of N-acetylglucosamine oligosaccharides}, author={John A. Rupley}, journal={Proceedings of the Royal Society of London. Series B. Biological Sciences}, year={1967}, volume={167}, pages={416 - 428} }
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.
28 Citations
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1H-NMR analysis of R114H and R114A indicated that the structural changes induced by the mutations were not restricted to the region surrounding Arg114, but rather extended to the aromatic side chains of Phe34 and Trp123, of which the signals are connected with each other through nuclear Overhauser effect (NOE) in the wild-type.
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