Conformational stability of calreticulin

Charlotte S Jørgensen; Christa Trandum; Nanna Larsen; L Rebekka Ryder; Michael Gajhede; Lars K Skov; Peter Højrup; Vibeke Barkholt; Gunnar Houen

doi:10.2174/0929866054696082

Conformational stability of calreticulin

Protein Pept Lett. 2005 Oct;12(7):687-93. doi: 10.2174/0929866054696082.

Authors

Charlotte S Jørgensen¹, Christa Trandum, Nanna Larsen, L Rebekka Ryder, Michael Gajhede, Lars K Skov, Peter Højrup, Vibeke Barkholt, Gunnar Houen

Affiliation

¹ Department of Research and Development, Statens Serum Institut, 2300 Copenhagen S, Denmark.

PMID: 16522185
DOI: 10.2174/0929866054696082

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Calcium / chemistry
Calcium / pharmacology
Calorimetry, Differential Scanning
Calreticulin / chemistry*
Calreticulin / metabolism*
Cations, Divalent / chemistry
Circular Dichroism
Humans
Hydrogen-Ion Concentration
Protein Conformation
Protein Denaturation
Protein Folding
Temperature

Substances

Calreticulin
Cations, Divalent
Calcium