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Discovery of Novel Cyclic Salt Bridge in Thermophilic Bacterial Protease and Study of its Sequence and Structure

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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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Acknowledgments

We are thankful to Dr. Pradipta Saha, Department of Microbiology, University of Burdwan, for his help and support.

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  1. Department of Microbiology, Raiganj University, Raiganj, WB, India

    Debanjan Mitra & Pradeep K. Das Mohapatra

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  1. Debanjan Mitra
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Contributions

D.M. conceived and designed the project. P.K.D.M. conducted initial manual verifications. Protein sequence and structure were identified by D.M. Analysis of those results was done by D.M. Draft of the manuscript was prepared by D.M. Final version of the manuscript was prepared by P.K.D.M. The whole work was done under the supervision of P.K.D.M.

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Correspondence to Pradeep K. Das Mohapatra.

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Mitra, D., Das Mohapatra, P.K. Discovery of Novel Cyclic Salt Bridge in Thermophilic Bacterial Protease and Study of its Sequence and Structure. Appl Biochem Biotechnol 193, 1688–1700 (2021). https://doi.org/10.1007/s12010-021-03547-3

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