Cysteine shotgun-mass spectrometry (CS-MS) reveals dynamic sequence of protein structure changes within mutant and stressed cells.

@article{Krieger2011CysteineSS,
  title={Cysteine shotgun-mass spectrometry (CS-MS) reveals dynamic sequence of protein structure changes within mutant and stressed cells.},
  author={Christine Carag Krieger and Xiuli An and Hsin-Yao Tang and Narla Mohandas and David W. Speicher and Dennis E Discher},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 20},
  pages={8269-74}
}
Questions of if and when protein structures change within cells pervade biology and include questions of how the cytoskeleton sustains stresses on cells--particularly in mutant versus normal cells. Cysteine shotgun labeling with fluorophores is analyzed here with mass spectrometry of the spectrin-actin membrane skeleton in sheared red blood cell ghosts from normal and diseased mice. Sheared samples are compared to static samples at 37 °C in terms of cell membrane intensity in fluorescence… CONTINUE READING

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