Conformational stability of calreticulin.
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.
Jørgensen
Charlotte S
CS
Department of Research and Development, Statens Serum Institut, 2300 Copenhagen S, Denmark.
Trandum
Christa
C
Larsen
Nanna
N
Ryder
L Rebekka
LR
Gajhede
Michael
M
Skov
Lars K
LK
Højrup
Peter
P
Barkholt
Vibeke
V
Houen
Gunnar
G
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
D037282:Calreticulin; D002413:Cations, Divalent; D002118:Calcium