Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry

@article{Lambert2012ProbingTT,
  title={Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry},
  author={Wietske Lambert and Gudrun Rutsdottir and Rasha Hussein and Katja Bernfur and Sven Kjellstr{\"o}m and Cecilia Emanuelsson},
  journal={Cell Stress and Chaperones},
  year={2012},
  volume={18},
  pages={75-85}
}
Small heat-shock protein chaperones are important players in the protein quality control system of the cell, because they can immediately respond to partially unfolded proteins, thereby protecting the cell from harmful aggregates. The small heat-shock proteins can form large polydisperse oligomers that are exceptionally dynamic, which is implicated in their function of protecting substrate proteins from aggregation. Yet the mechanism of substrate recognition remains poorly understood, and… CONTINUE READING

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tection of crosslinks within and between proteins by LC - MALDI - TOFTOF and the software FINDX to reduce the MSMS - data to acquire for validation

  • F Stengel, AJ Baldwin, +6 authors JL Benesch
  • PLoS ONE
  • 2012

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