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1. Clusters of lysozyme in aqueous solutions

   https://doi.org/10.1103/PhysRevE.98.032419  

   Baumketner, A.; Cai, W. (September 2018, Physical Review E)
2. Templated Synthesis of Copper Nanoclusters with a Hybrid Lysozyme-Polymer Material for Enhanced Fluorescence

   https://doi.org/10.1021/acs.bioconjchem.4c00058  

   Larkin, James O; Cheng, Zhihua; Arefeayne, Yafet; Segatori, Laura; Jones, Matthew R; Ball, Zachary T (May 2024, Bioconjugate Chemistry)

   Hybrid materials that combine organic polymers and biomacromolecules offer unique opportunities for precisely controlling 3D chemical environments. Although biological or organic templates have been separately used to control the growth of inorganic nanoclusters, hybrid structures represent a relatively unexplored approach to tailoring nanocluster properties. Here, we demonstrate that a molecularly defined lysozyme–polymer resin material acts as a structural scaffold for the synthesis of copper nanoclusters (CuNCs) with well controlled size distributions. The resulting CuNCs have significantly enhanced fluorescence compared with syntheses based on polymeric or biological templates alone. The synergistic approach described here is appealing for the synthesis of biocompatible fluorescent labels with improved photostability. 

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3. Effects of Protein Unfolding on Aggregation and Gelation in Lysozyme Solutions

   https://doi.org/10.3390/biom10091262  

   Nikfarjam, Shakiba; Jouravleva, Elena V.; Anisimov, Mikhail A.; Woehl, Taylor J. (September 2020, Biomolecules)

   null (Ed.)

   In this work, we investigate the role of folding/unfolding equilibrium in protein aggregation and formation of a gel network. Near the neutral pH and at a low buffer ionic strength, the formation of the gel network around unfolding conditions prevents investigations of protein aggregation. In this study, by deploying the fact that in lysozyme solutions the time of folding/unfolding is much shorter than the characteristic time of gelation, we have prevented gelation by rapidly heating the solution up to the unfolding temperature (~80 °C) for a short time (~30 min.) followed by fast cooling to the room temperature. Dynamic light scattering measurements show that if the gelation is prevented, nanosized irreversible aggregates (about 10–15 nm radius) form over a time scale of 10 days. These small aggregates persist and aggregate further into larger aggregates over several weeks. If gelation is not prevented, the nanosized aggregates become the building blocks for the gel network and define its mesh length scale. These results support our previously published conclusion on the nature of mesoscopic aggregates commonly observed in solutions of lysozyme, namely that aggregates do not form from lysozyme monomers in their native folded state. Only with the emergence of a small fraction of unfolded proteins molecules will the aggregates start to appear and grow. 

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4. Designing Highly Thermostable Lysozyme–Copolymer Conjugates: Focus on Effect of Polymer Concentration

   https://doi.org/10.1021/acs.biomac.8b00027  

   Choudhury, Chandan Kumar; Tu, Sidong; Luzinov, Igor; Minko, Sergiy; Kuksenok, Olga (March 2018, Biomacromolecules)
5. Graph Clustering Analyses of Discontinuous Molecular Dynamics Simulations: Study of Lysozyme Adsorption on a Graphene Surface

   https://doi.org/10.1021/acs.langmuir.2c01331  

   Chen, Jing; Xu, Enze; Wei, Yong; Chen, Minghan; Wei, Tao; Zheng, Size (September 2022, Langmuir)