OCAM: a new tool for studying the oligomeric diversity of MscL channels.

@article{Gandhi2011OCAMAN,
  title={OCAM: a new tool for studying the oligomeric diversity of MscL channels.},
  author={Chris S. Gandhi and Troy A. Walton and Douglas C Rees},
  journal={Protein science : a publication of the Protein Society},
  year={2011},
  volume={20 2},
  pages={313-26}
}
We have developed a new technique to study the oligomeric state of proteins in solution. OCAM or Oligomer Characterization by Addition of Mass counts protein subunits by selectively shaving a protein mass tag added to a protein subunit via a short peptide linker. Cleavage of each mass tag reduces the total mass of the protein complex by a fixed amount. By performing limited proteolysis and separating the reaction products by size on a blue native PAGE gel, a ladder of reaction products… CONTINUE READING

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References

Publications referenced by this paper.
Showing 1-10 of 41 references

Crystal structure of the extracellular domain of a bacterial ligand-gated ion channel

H Nury, N Bocquet, +4 authors M Delarue
J Mol Biol • 2010

Gating-associated conformational changes in the mechanosensitive channel MscL.

Proceedings of the National Academy of Sciences of the United States of America • 2008

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