Conformational stability of calreticulin.

@article{Jrgensen2005ConformationalSO,
  title={Conformational stability of calreticulin.},
  author={Charlotte Svaerke J\orgensen and Christa Trandum and Nanna H Larsen and Lisa Rebekka Ryder and Michael Gajhede and Lars K. Skov and Peter H\ojrup and Vibeke Barkholt and Gunnar Houen},
  journal={Protein and peptide letters},
  year={2005},
  volume={12 7},
  pages={687-93}
}
The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (Tm) increased from 31 degrees C at pH 5 to 51 degrees C at pH 9, but electrophoretic analysis revealed that calreticulin oligomerized instead of unfolding. Structural analyses showed that the single C-terminal alpha-helix was of major importance to the conformational stability of calreticulin. 

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