Compressibility and Volume Changes of Lysozyme due to Inhibitor Binding

• Kunihiko Gekko

  Department of Materials Science, Faculty of Science, Hiroshima University

• Keigo Yamagami

  Department of Materials Science, Faculty of Science, Hiroshima University

Abstract

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.

Journal

• Chemistry Letters

  Chemistry Letters 27 (8), 839-840, 1998-08-01

  Oxford University Press (OUP)

Keywords

• General Chemistry

Details

• CRID: 1360002219109560704
• NII Article ID: 10004484834
• NII Book ID: AA00603318
• DOI: 10.1246/cl.1998.839
• ISSN: 13480715
• ISSN: 03667022
• Web Site: https://academic.oup.com/chemlett/article-pdf/27/8/839/56072473/cl.1998.839.pdf
• Data Source:
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  • CiNii Articles