The effect of Met-->Leu mutations on calmodulin's ability to activate cyclic nucleotide phosphodiesterase.

@article{Zhang1994TheEO,
  title={The effect of Met-->Leu mutations on calmodulin's ability to activate cyclic nucleotide phosphodiesterase.},
  author={Mingjie Zhang and Mi Li and Jerry H. C. Wang and Hans J. Vogel},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 22},
  pages={15546-52}
}
Calmodulin (CaM) has two hydrophobic surface patches that are particularly rich in Met residues, and these are the major contact areas where CaM interacts with its target enzymes. The amino acid Leu has been introduced by site-directed mutagenesis to replace all the Met residues in CaM. All nine individual Met-->Leu mutants of CaM as well as some double and quadruple mutants were expressed in Escherichia coli. All mutants could be purified by calcium-dependent hydrophobic affinity… CONTINUE READING

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