The Mutator S (MutS) protein is a crucial part of the DNA mismatch repair (MMR) pathway. MutS scans genomic DNA for insertion deletion loops, and when a mutation is encountered, the protein undergoes ATP hydrolysis which triggers a conformational change that allows for the protein to initiate the repair sequence. It measures approximately 100 Å between the active sites, thus raising the question of how ATP hydrolysis conveys an allosteric signal to the DNA binding site at such a distance. The mechanism by which allosteric communication occurs has been investigated previously using statistical coupling analysis (SCA) and limited molecular dynamics (MD) simulations to identify the key residues in communication. This work focuses on further characterizing the wild type and key mutant systems of MutS using MD simulations and MD based Markov State Models (MSMs) to gain insight into the allosteric nature of the protein.
"},{"label":"Degree","value":["Bachelor of Arts with Departmental Honors"]},{"label":"Administrative Note","value":"Drupal Node ID: 24252