Improving protein solubility through rationally designed amino acid replacements: solubilization of the trimethoprim-resistant type S1 dihydrofolate reductase.

@article{Dale1994ImprovingPS,
  title={Improving protein solubility through rationally designed amino acid replacements: solubilization of the trimethoprim-resistant type S1 dihydrofolate reductase.},
  author={Glenn E. Dale and Clemens Broger and H. Hans Langen and Allan D'arcy and Dietrich Stueber},
  journal={Protein engineering},
  year={1994},
  volume={7 7},
  pages={933-9}
}
In recent years resistance to the antibacterial agent trimethoprim (Tmp) has become more widespread and several Tmp-resistant (Tmpr) dihydrofolate reductases (DHFRs) have been described from Gram-negative bacteria. In staphylococci, however, only one Tmpr DHFR (type S1 DHFR) has been found so far, and this is located on transposon Tn4003. To help understand the mechanism of resistance, we are interested in determining the 3-D structure of the recombinant enzyme produced in Escherichia coli… CONTINUE READING
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