Noncovalent interaction energies in covalent complexes: TEM-1 beta-lactamase and beta-lactams.

@article{Wang2002NoncovalentIE,
  title={Noncovalent interaction energies in covalent complexes: TEM-1 beta-lactamase and beta-lactams.},
  author={Xiaojun Wang and George Minasov and Brian K. Shoichet},
  journal={Proteins},
  year={2002},
  volume={47 1},
  pages={86-96}
}
The class A beta-lactamase TEM-1 is a key bacterial resistance enzyme against beta-lactam antibiotics, but little is known about the energetic bases for complementarity between TEM-1 and its inhibitors. Most inhibitors form a covalent adduct with the catalytic Ser70, making the measurement of equilibrium constants, and hence interaction energies, technically difficult. This study evaluates noncovalent interactions within covalent complexes by examining the differential stability of TEM-1 and… CONTINUE READING
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