Maiti Arnab, Dey Krishna Kanti
Laboratory of Soft and Living Materials, Department of Physics, Indian Institute of Technology Gandhinagar Palaj Gandhinagar Gujarat 382055 India
Nanoscale Adv. 2025 Jul 29. doi: 10.1039/d5na00405e.
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.
蛋白质在动态环境中发挥作用，其中相互作用和波动会影响其结构和功能。了解这些因素如何影响酶的稳定性，对于基础生物学和实际应用都至关重要。在这里，我们研究了蛋白质-蛋白质相互作用和非热活性波动在酶构象动力学和催化活性中的作用。我们的研究结果表明，在密集悬浮液中，酶的催化活性和结构完整性能在较长时间内得以保持。此外，我们观察到酶催化反应产生的机械波动有助于在更长的时间尺度上维持酶活性。
