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dc.contributor.authorAvery, Christopher
dc.contributor.authorFarmer, Jenny
dc.contributor.authorTsilimigras, Matthew C. B.
dc.contributor.authorDavid, Charles
dc.contributor.authorLivesay, Dennis R.
dc.contributor.authorJacobs, Donald J.
dc.identifier.citationAvery, Christopher; Farmer, Jenny; Tsilimigras, Matthew C. B.; David, Charles; Livesay, Dennis R.; Jacobs, Donald J. 2019. Characterizing dynamical differences between TEM-1 and TEM-52 beta-lactamases. Biophysical Journal, vol. 116:no. 3:S1:pp 343aen_US
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractBeta-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.en_US
dc.publisherCell Pressen_US
dc.relation.ispartofseriesBiophysical Journal;v.116:no.3:S1
dc.subjectMeeting abstracten_US
dc.titleCharacterizing dynamical differences between TEM-1 and TEM-52 beta-lactamasesen_US
dc.rights.holder© 2019, Elsevieren_US

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