Compressibility and volume changes of lysozyme due to inhibitor binding

摘要

The adiabatic compressibility and partial specific volume of hen egg-white lysozyme, which were determined by the sound velocity and density measurements at 25 degrees 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. [References: 12]