Conformational stability of calreticulin

Research output: Contribution to journalJournal articleResearchpeer-review

  • Charlotte S Jørgensen
  • Christa Trandum
  • Nanna Brink Larsen
  • L Rebekka Ryder
  • Gajhede, Michael
  • Lars Skov
  • Peter Højrup
  • Vibeke Barkholt
  • Gunnar Houen
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.
Original languageEnglish
JournalProtein and Peptide Letters
Issue number7
Pages (from-to)687-93
Number of pages7
Publication statusPublished - 2005

    Research areas

  • Calcium, Calorimetry, Differential Scanning, Calreticulin, Cations, Divalent, Circular Dichroism, Humans, Hydrogen-Ion Concentration, Protein Conformation, Protein Denaturation, Protein Folding, Temperature

ID: 40766666