Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda

Area of Science:

• Structural biology
• Biochemistry
• Molecular biophysics

Background:

• Lambda lysozyme, an 18 kDa globular protein, shares structural domains and catalytic residue placement with other lysozymes.
• Unlike hen egg-white lysozyme, lambda lysozyme lacks disulfide bridges, making it a valuable model for protein folding studies.
• Understanding the role of disulfide bonds in protein refolding is critical in biochemistry.

Purpose of the Study:

• To determine the backbone resonance assignments for lambda lysozyme using multidimensional NMR.
• To establish a foundation for investigating the protein's refolding pathway.
• To compare folding properties with hen egg-white lysozyme, elucidating disulfide bond roles.

Main Methods:

• Heteronuclear multidimensional Nuclear Magnetic Resonance (NMR) spectroscopy was employed.
• Proton (1H), Carbon-13 (13C), and Nitrogen-15 (15N) backbone resonance assignments were obtained.
• NMR was used to monitor pulse-labelling hydrogen/deuterium exchange experiments.

Main Results:

• Complete (1)H, (13)C, and (15)N backbone resonance assignments for lambda lysozyme were successfully determined.
• These assignments serve as essential data for subsequent structural and dynamic analyses.
• The data provides a basis for future studies on lambda lysozyme's folding and refolding mechanisms.

Conclusions:

• The reported NMR assignments are fundamental for detailed investigations into lambda lysozyme's protein folding.
• This work facilitates comparative studies with other lysozymes, highlighting the influence of disulfide bonds.
• Future research will utilize these assignments to explore refolding pathways via hydrogen/deuterium exchange NMR.