Compressibility and Volume Changes of Lysozyme due to Inhibitor Binding
The adiabatic compressibility and partial specific volume of hen egg-white lysozyme, which were determined by the sound velocity and density measurements at 25 °C, decreased by addition of its inhibitors, N-acetyl-D-glucosamine oligomers, in the order of monomer > dimer > trimer. This result demonstrates that the inhibitor binding induces the atomic packing in the cleft of the active site to diminish the structural fluctuation of the protein.
- Chemistry letters
Chemistry letters 1998(8), 839-840, 1998-08-05
The Chemical Society of Japan