Polydispersity of a mammalian chaperone: Mass spectrometry reveals the population of oligomers in αB-crystallin

@article{Aquilina2003PolydispersityOA,
  title={Polydispersity of a mammalian chaperone: Mass spectrometry reveals the population of oligomers in $\alpha$B-crystallin},
  author={John A. Aquilina and Justin L. P. Benesch and Orval A. Bateman and Christine Slingsby and Carol V. Robinson},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100},
  pages={10611 - 10616}
}
The quaternary structure of the polydisperse mammalian chaperone αB-crystallin, a member of the small heat-shock protein family, has been investigated by using electrospray mass spectrometry. The intact assemblies give rise to mass spectra that are complicated by the overlapping of charge states from the different constituent oligomers. Therefore, to determine which oligomers are formed by this protein, tandem mass spectrometry experiments were performed. The spectra reveal a distribution… 

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