Abstract

Protein-protein interactions underlie supramolecular self-formation structures (including enzymes). Nowadays, they have a crucial role, as they contribute to the creation of biological substances with a certain function. Due to their unique properties, proteins, and enzymes have been widely studied in the last few years and their important roles in health and various diseases have been proven from this point of view, many enzymes are characterized by the process of self-formation ("self-assembly") depending on different conditions. Such an enzyme is arginase (including isoenzymes I and II), which can be considered as a biomarker clarifying the pathological conditions of the organism. Based on this, we aimed to create simple fractal models and study the changes in oligomeric structure (depending on pH and time) during the reversible inactivation of rabbit arginase I and II and elucidate the unique aspects of "self-assembly". We have shown that the "false" oligomers formed in the process of protein "self-assembly" in vitro can appear as intermediate structures endowed with enzymatic activity.

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