Conformational stability of calreticulin

C.S. Jørgensen, C. Trandum, N. Larsen, L.R. Ryder, M. Gajhede, L.K. Skov, P. Højrup, Vibeke Barkholt, G. Houen

    Research output: Contribution to journalJournal articleResearchpeer-review


    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 languageEnglish
    JournalProtein and Peptide Letters
    Issue number7
    Pages (from-to)687-693
    Publication statusPublished - 2005


    • oligomerization
    • stability
    • calreticulin
    • conformation
    • heat shock protein


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