Hait Suman, Basu Sudipto, Kundu Sudip
Department of Biophysics, Molecular Biology and Bioinformatics, University of Calcutta, Kolkata, India.
J Biomol Struct Dyn. 2023 Mar;41(5):1745-1752. doi: 10.1080/07391102.2021.2024258. Epub 2022 Jan 7.
Proteins from thermophilic organisms are a matter of immense interest for decades because of its application in fields like de-novo protein design, thermostable variants of biocatalysts etc. Previous studies have found several sequence and structural adaptations related to thermal stability, while charge reversal study remains ignored. Here we address whether charge reversal mutations naturally occur in mesophilic-thermophilic/hyperthermophilic orthologous proteins. Do they contribute to thermal stability? Our systematic study on 1550 mesophilic-thermophilic/hyperthermophilic orthologous protein pairs with remarkable structural and topological similarity, shows gain in coulombic interaction energy in thermophilic/hyperthermophilic proteins at short range associated with partially exposed and buried charge reversal mutations, which may enhance thermostability. Our findings call forth its application in future protein engineering studies. Communicated by Ramaswamy H. Sarma.
几十年来，嗜热生物的蛋白质一直备受关注，因为其在从头蛋白质设计、生物催化剂的热稳定变体等领域有应用。先前的研究发现了一些与热稳定性相关的序列和结构适应性变化，而电荷反转研究仍被忽视。在这里，我们探讨电荷反转突变是否自然发生在中温-嗜热/超嗜热直系同源蛋白中。它们是否有助于热稳定性？我们对1550对具有显著结构和拓扑相似性的中温-嗜热/超嗜热直系同源蛋白对进行的系统研究表明，嗜热/超嗜热蛋白在短程内库仑相互作用能增加，这与部分暴露和埋藏的电荷反转突变有关，这可能会增强热稳定性。我们的发现促使其在未来的蛋白质工程研究中得到应用。由拉马斯瓦米·H·萨尔马传达。
