Preserving enzyme conformation and catalytic efficiency in crowded and active environments

Abstract

Proteins operate in dynamic environments where interactions and fluctuations influence their structure and function. Understanding how these factors contribute to enzyme stability is essential for both fundamental biology and practical applications. Here, we investigate the role of protein–protein interactions and non-thermal active fluctuations in enzyme conformational dynamics and catalytic activity. Our findings reveal that in a dense suspension, enzyme catalytic activity and structural integrity are preserved for extended periods. Additionally, we observed that mechanical fluctuations generated by enzyme catalytic reactions help sustain enzymatic activity over longer timescales.