title: Conformational stability of calreticulin.
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.
authors.affiliation: Department of Research and Development, Statens Serum Institut, 2300 Copenhagen S, Denmark.
authors.forename: Charlotte S
authors.initials: CS
authors.lastname: Jørgensen
authors.forename: Christa
authors.initials: C
authors.lastname: Trandum
authors.forename: Nanna
authors.initials: N
authors.lastname: Larsen
authors.forename: L Rebekka
authors.initials: LR
authors.lastname: Ryder
authors.forename: Michael
authors.initials: M
authors.lastname: Gajhede
authors.forename: Lars K
authors.initials: LK
authors.lastname: Skov
authors.forename: Peter
authors.initials: P
authors.lastname: Højrup
authors.forename: Vibeke
authors.initials: V
authors.lastname: Barkholt
authors.forename: Gunnar
authors.initials: G
authors.lastname: Houen
mesh_terms: D002118:Calcium / Q000737:chemistry / Q000494:pharmacology; D002152:Calorimetry, Differential Scanning; D037282:Calreticulin / Q000737:chemistry* / Q000378:metabolism*; D002413:Cations, Divalent / Q000737:chemistry; D002942:Circular Dichroism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013696:Temperature
chemical_list: D037282:Calreticulin; D002413:Cations, Divalent; D002118:Calcium