%0 Journal Article
%T Effect of the Lys62Ala Mutation on the Thermal Stability of BstHPr Protein by Molecular Dynamics.
%A Martínez-Zacarias AC
%A López-Pérez E
%A Alas-Guardado SJ
%J Int J Mol Sci
%V 25
%N 12
%D 2024 Jun 7
%M 38928023
%F 6.208
%R 10.3390/ijms25126316
%X We analyzed the thermal stability of the BstHPr 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 BstHPrm protein were compared with those of the wild-type thermophilic BstHPr protein and the mesophilic BsHPr 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 BstHPr protein.