ArticleApplied biochemistry and biotechnology2021
Discovery of Novel Cyclic Salt Bridge in Thermophilic Bacterial Protease and Study of its Sequence and Structure.
Article in Applied biochemistry and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 22 citations in OpenAlex.
- AnFrontiers in chemistry · 2026Article
- Article
- Potentiality of bioactive compounds as inhibitor of M protein and F protein function of human respiratory syncytial virus.In silico pharmacology · 2024Article
- Modeling the role of charged residues in thermophilic proteins by rotamer and dynamic cross correlation analysis.Journal of molecular modeling · 2023Article
- In silico comparative structural and compositional analysis of glycoproteins of RSV to study the nature of stability and transmissibility of RSV A.Systems microbiology and biomanufacturing · 2023Article
- Intra-protein interactions of SARS-CoV-2 and SARS: a bioinformatic analysis for plausible explanation regarding stability, divergency, and severity.Systems microbiology and biomanufacturing · 2022Article
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2 authors at 1 institution in 1 country.
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Abstract
The plausible explanation behind the stability of thermophilic protein is still yet to be defined more clearly. Here, an in silico study has been undertaken by investigating the sequence and structure of protease from thermophilic (tPro) bacteria and mesophilic (mPro) bacteria. Results showed that charged and uncharged polar residues have higher abundance in tPro. In extreme environment, the tPro is stabilized by high number of isolated and network salt bridges. A novel cyclic salt bridge is also found in a structure of tPro. High number of metal ion-binding site also helps in protein stabilization of thermophilic protease. Aromatic-aromatic interactions also play a crucial role in tPro stabilization. Formation of long network aromatic-aromatic interactions also first time reported here. Finally, the present study provides a major insight with a newly identified cyclic salt bridge in the stability of the enzyme, which may be helpful for protein engineering. It is also used in industrial applications for human welfare.
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