A quantitative strategy to detect changes in accessibility of protein regions to chemical modification on heterodimerization.

@article{Dreger2009AQS,
  title={A quantitative strategy to detect changes in accessibility of protein regions to chemical modification on heterodimerization.},
  author={Mathias Dreger and Bo Wah Leung and George G. Brownlee and Tao Deng},
  journal={Protein science : a publication of the Protein Society},
  year={2009},
  volume={18 7},
  pages={1448-58}
}
We describe a method for studying quantitative changes in accessibility of surface lysine residues of the PB1 subunit of the influenza RNA polymerase as a result of association with the PA subunit to form a PB1-PA heterodimer. Our method combines two established methods: (i) the chemical modification of surface lysine residues of native proteins by N-hydroxysuccinimidobiotin (NHS-biotin) and (ii) the stable isotope labeling of amino acids in cell culture (SILAC) followed by tryptic digestion… CONTINUE READING

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Subunit-specific protein footprinting reveals significant structural rearrangements and a role for N-terminal Lys-14 of Dreger et al. PROTEIN SCIENCE VOL 18:1448—1458

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