Beta-lactamase, produced in bacteria, defends against beta-lactam antibiotics such as penicillin and cephalosporins by hydrolyzing the beta-lactam ring. This is a primary cause of antibiotic resistance to beta-lactam antibiotics. The most common beta-lactamase, TEM-1, hydrolyze penicillin and first-generation cephalosporins. Within the TEM family alone there are over 400 sequences differing from the TEM-1 sequence by point mutations. Some of these mutations have conferred the beta-lactamase enzymes with extended substrate specificity which allow the hydrolysis of a wider range of beta-lactam antibiotics. These enzymes are known as extended spectrum beta-lactamases (ESBL), and they present a major challenge to the design of new antibiotics While the chemical mechanism of beta-lactamase resistance is well-known, the dynamics of sequence mutants conferring extended spectrum activity is not yet understood. In this work we aim to characterize differences in dynamics.