Conformational stability of calreticulin
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Conformational stability of calreticulin. / Jørgensen, Charlotte S; Trandum, Christa; Larsen, Nanna Brink; Ryder, L Rebekka; Gajhede, Michael; Skov, Lars; Højrup, Peter; Barkholt, Vibeke; Houen, Gunnar.
In: Protein and Peptide Letters, Vol. 12, No. 7, 2005, p. 687-93.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Conformational stability of calreticulin
AU - Jørgensen, Charlotte S
AU - Trandum, Christa
AU - Larsen, Nanna Brink
AU - Ryder, L Rebekka
AU - Gajhede, Michael
AU - Skov, Lars
AU - Højrup, Peter
AU - Barkholt, Vibeke
AU - Houen, Gunnar
PY - 2005
Y1 - 2005
N2 - 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.
AB - 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.
KW - Calcium
KW - Calorimetry, Differential Scanning
KW - Calreticulin
KW - Cations, Divalent
KW - Circular Dichroism
KW - Humans
KW - Hydrogen-Ion Concentration
KW - Protein Conformation
KW - Protein Denaturation
KW - Protein Folding
KW - Temperature
M3 - Journal article
C2 - 16522185
VL - 12
SP - 687
EP - 693
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
SN - 0929-8665
IS - 7
ER -
ID: 40766666