The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (T-m) 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 a-helix was of major importance to the conformational stability of calreticulin.
|Journal||Protein and Peptide Letters|
|Publication status||Published - 2005|
- heat shock protein