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Protein & Peptide Letters

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

DOI: 10.2174/0929866054696082

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Conformational Stability of Calreticulin

Page: [687 - 693] Pages: 7

  • * (Excluding Mailing and Handling)

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.

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