Conformational Stability of Calreticulin

Title: Conformational Stability of Calreticulin

Volume: 12 Issue: 7

Author(s): Charlotte S. Jorgensen, Christa Trandum, Nanna Larsen, L. R. Ryder, Michael Gajhede, Lars K. Skov, Peter Hojrup, Vibeke Barkholt and Gunnar Houen

Affiliation:

Keywords: calreticulin, conformation, stability, oligomerization, heat shock protein

Abstract: The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (Tm) increased from 31°C at pH 5 to 51°C at pH 9, but electrophoretic analysis revealed that calreticulin oligomerized instead of unfolding. Structural analyses showed that the single C-terminal α-helix was of major importance to the conformational stability of calreticulin.

Cite this article as:

Jorgensen S. Charlotte, Trandum Christa, Larsen Nanna, Ryder R. L., Gajhede Michael, Skov K. Lars, Hojrup Peter, Barkholt Vibeke and Houen Gunnar, Conformational Stability of Calreticulin, Protein & Peptide Letters 2005; 12 (7) . https://dx.doi.org/10.2174/0929866054696082