A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin.

@article{Treweek2010AQN,
  title={A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin.},
  author={Teresa M. Treweek and Agata Rekas and Mark J Walker and John A Carver},
  journal={Experimental eye research},
  year={2010},
  volume={91 5},
  pages={691-9}
}
The principal lens proteins αA- and αB-crystallin are members of the small heat-shock protein (sHsp) family of molecular chaperone proteins. Via their chaperone action, αA- and αB-crystallin play an important role in maintaining lens transparency by preventing crystallin protein aggregation and precipitation. αB-crystallin is found extensively extralenticularly where it is stress inducible and acts as a chaperone to facilitate general protein stabilization. The structure of either αA- or αB… CONTINUE READING

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