{Reference Type}: Journal Article
{Title}: Effect of the Lys62Ala Mutation on the Thermal Stability of BstHPr Protein by Molecular Dynamics.
{Author}: Martínez-Zacarias AC;López-Pérez E;Alas-Guardado SJ;
{Journal}: Int J Mol Sci
{Volume}: 25
{Issue}: 12
{Year}: 2024 Jun 7
{Factor}: 6.208
{DOI}: 10.3390/ijms25126316
{Abstract}: 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.