Corpus ID: 19895060

Functional analyses of AmpC beta-lactamase through differential stability.

@article{Beadle1999FunctionalAO,
  title={Functional analyses of AmpC beta-lactamase through differential stability.},
  author={B. Beadle and S. McGovern and A. Patera and B. Shoichet},
  journal={Protein science : a publication of the Protein Society},
  year={1999},
  volume={8 9},
  pages={
          1816-24
        }
}
Despite decades of intense study, the complementarity of beta-lactams for beta-lactamases and penicillin binding proteins is poorly understood. For most of these enzymes, beta-lactam binding involves rapid formation of a covalent intermediate. This makes measuring the equilibrium between bound and free beta-lactam difficult, effectively precluding measurement of the interaction energy between the ligand and the enzyme. Here, we explore the energetic complementarity of beta-lactams for the beta… Expand
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