Investigating the Conformational Dynamics of the Enzyme Guanylate Kinase from Mutations at Two Locations

In this study, we look at the conformational dynamics of the enzyme Guanylate Kinase (GK), as well as 3 mutants of the enzyme. Achieving mutations with significant functional change to the protein is generally the result of many changes to the sequence of amino acids, but in the case of GK, we see that with only two mutations have caused changes in the enzyme activity. This mutant is the result of Alanines in residue 175 and 176 being changed to Glycine. Taking use of molecular dynamics, docking, and free energy profiles we provide a full description of the conformational changes of the three mutants.