Lysozymes from different organisms: chirality of helical structures, amino acids composition and protein stability

Lysozyme is a vital enzyme that plays a crucial role in the immune system by defending against bacterial infections. Due to its potent antimicrobial activity, stability, and safety, lysozyme is widely utilized in various fields including medicine, food preservation, and biotechnology. This paper offers a comprehensive analysis of lysozymes derived from different organisms, focusing on their structural features, amino acid composition, and the factors influencing their stability. This paper focuses mainly on analyzing helical structures of lysozyme, especially α-helices, because they represent the most abundant secondary structure element (1/3 of lysozyme primary structure). One key aspect of this investigation is the chirality of protein structural elements, which is defined as the incompatibility of an entity with its mirror image. The aim of this work is to establish the relationship between chirality of lysozyme helical structures, their energy and stability. The study emphasizes the importance of amino acid interactions, structural motifs such as salt bridges and disulfide bonds, and the role of chirality in analyzed structures. These insights are valuable for advancing protein engineering efforts aimed at enhancing enzyme stability and designing novel therapeutics. Overall, understanding the structural determinants of lysozyme allows to develop more effective antimicrobial agents and biotechnological applications.