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The steady state and time-resolved fluorescence studies on the lysozyme-ligand interaction
S Yamashita1, E Nishimoto, N Yamasaki
1Institute of Biophysics, Faculty of Agricutlure, Kyushu University, Fukuoka, Japan.
Bioscience, Biotechnology, and Biochemistry
|July 1, 1995
Summary
Hen egg-white lysozyme undergoes conformational changes upon binding with tri-N-acetyl-D-glucosamine. This ligand interaction influences tryptophan residues and the hydrophobic matrix, altering protein structure and dynamics.
Area of Science:
- Biochemistry
- Structural Biology
- Spectroscopy
Background:
- Hen egg-white lysozyme is a well-studied enzyme.
- Understanding protein-ligand interactions is crucial for drug design and enzyme engineering.
Purpose of the Study:
- To investigate the conformational changes in hen egg-white lysozyme induced by tri-N-acetyl-D-glucosamine.
- To elucidate the impact of ligand binding on the protein's structural dynamics.
Main Methods:
- Steady-state and time-resolved fluorescence spectroscopy.
- Analysis of fluorescence decay kinetics across full spectral regions.
- Spectral analysis of lysozyme-ligand complex.
Main Results:
- Ligand binding affects Trp62, Trp108, and the hydrophobic matrix region.
- Intramolecular distance between Trp108 and Glu35 varies with pH.
- Fluctuational motions of Trp28 and Trp111 are restricted.
Conclusions:
- Tri-N-acetyl-D-glucosamine binding induces significant conformational alterations in hen egg-white lysozyme.
- The effects of ligand binding propagate beyond the immediate binding site.
- pH-dependent structural dynamics near the binding site are observed.