Conformational stability of calreticulin
Research output: Contribution to journal › Journal article › Research › peer-review
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.
|Journal||Protein and Peptide Letters|
|Number of pages||7|
|Publication status||Published - 2005|
- Calcium, Calorimetry, Differential Scanning, Calreticulin, Cations, Divalent, Circular Dichroism, Humans, Hydrogen-Ion Concentration, Protein Conformation, Protein Denaturation, Protein Folding, Temperature