Effect of the Lys62Ala Mutation on the Thermal Stability of Bst HPr Protein by Molecular Dynamics
We analyzed the thermal stability of the HPr protein through the site-directed point mutation Lys62 replaced by Ala residue using molecular dynamics simulations at five different temperatures: 298, 333, 362, 400, and 450 K, for periods of 1 μs and in triplicate. The results from the mutant thermophi...
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Published in | International journal of molecular sciences Vol. 25; no. 12 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Switzerland
07.06.2024
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Subjects | |
Online Access | Get full text |
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Summary: | We analyzed the thermal stability of the
HPr protein through the site-directed point mutation Lys62 replaced by Ala residue using molecular dynamics simulations at five different temperatures: 298, 333, 362, 400, and 450 K, for periods of 1 μs and in triplicate. The results from the mutant thermophilic
HPrm protein were compared with those of the wild-type thermophilic
HPr protein and the mesophilic
HPr protein. Structural and molecular interaction analyses show that proteins lose stability as temperature increases. Mutant and wild-type proteins behave similarly up to 362 K. However, at 400 K the mutant protein shows greater structural instability, losing more buried hydrogen bonds and exposing more of its non-polar residues to the solvent. Therefore, in this study, we confirmed that the salt bridge network of the Glu3-Lys62-Glu36 triad, made up of the Glu3-Lys62 and Glu36-Lys62 ion pairs, provides thermal stability to the thermophilic
HPr protein. |
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ISSN: | 1422-0067 |