Site-directed sulfhydryl labeling of helix IX in the lactose permease of Escherichia coli.

@article{Zhang2003SitedirectedSL,
  title={Site-directed sulfhydryl labeling of helix IX in the lactose permease of Escherichia coli.},
  author={Wei Zhang and Yonglin Hu and H Ronald Kaback},
  journal={Biochemistry},
  year={2003},
  volume={42 17},
  pages={4904-8}
}
Site-directed sulfhydryl modification of transmembrane helix IX in the lactose permease of Escherichia coli was studied in right-side-out membrane vesicles with the thiol-specific reagents N-[(14)C]ethylmaleimide (NEM) and methanethiosulfonate ethylsulfonate (MTSES) which are permeant and impermeant, respectively. Out of approximately 20 mutants with a single Cys residue at each position in the helix, only five mutants label with NEM. (i) Cys residues at positions 291, 308, and 310 label at 25… CONTINUE READING

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