A Nuclear Magnetic Resonance Study of the Inhibition of Lysozyme by N-Acetyl-D-glucosamine and Di-N-acetyl-D-glucosamine

The rate constants k, and k, for N-acetyl-a-and --Dglucosamine and di-N-acetyl-D-glucosamine exchanging with lysozyme have been determined by nuclear magnetic resonance methods, along with the chemical shifts of the acetyl proton resonances upon binding to lysozyme. The results suggest that the binding of N-acetyl-/3-D-glucosamine to lysozyme is significantly different from that of other monosaccharide inhibitors, that the value of k, for monosaccharide inhibitors is significantly different from that for the di-and trisaccharide, and that the phenomenon measured by nuclear magnetic resonance methods is the same as that measured by temperature jump methods.