Thermal dynamics of RNase A: unravelling interactions across varied temperatures in an in-silico exploration

Abstract

RNase A stands as a pivotal molecule due to its multifaceted significance across diverse domains. Its unique enzymatic properties and well-characterized structure make it a model for studying protein folding, enzymatic catalysis, and the intricate relationship between structure and function in proteins. Beyond research, RNase A and its derivatives exhibit promising potential in cancer therapy, showcasing cytotoxic effects on tumour cells. Temperature-induced changes in proteins are pivotal as they profoundly influence their structure, function, and applicability across diverse domains. These alterations can significantly impact protein folding, stability, and enzymatic activity, crucial for their biological functions. Specifically, the study delves into the interactions of various ligands, such as A3P, ATP, trehalose, sucrose, glucosylglycerol, and ribonuclease inhibitor, with RNase A across a range of temperatures using different computational methods. Among the ligands tested, A3P, ATP, and trehalose exhibited robust interactions with RNase A across diverse thermal conditions, suggesting their potential role in modulating RNase A's behaviour. Moreover, the investigation underscores temperature-sensitive interactions between RNase A and ribonuclease inhibitor, revealing potential therapeutic implications for modulating cytotoxic effects while preserving thermal stability. This study investigates the influence of temperature on flexibility, stability, and function on RNase A which is explored through computational simulations and molecular dynamics studies. The insights obtained from this study provide a deeper understanding of molecular relationships between diverse ligands and proteins across varying temperatures, suggesting promising avenues for future therapeutic applications.

URN:NBN:sciencein.btl.2024.v11.903