Abstract
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.
Original language | English |
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Journal | Protein and Peptide Letters |
Volume | 12 |
Issue number | 7 |
Pages (from-to) | 687-693 |
ISSN | 0929-8665 |
Publication status | Published - 2005 |
Keywords
- oligomerization
- stability
- calreticulin
- conformation
- heat shock protein