Conformational Stability of Calreticulin
Abstract:The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (Tm) increased from 31°C at pH 5 to 51°C at pH 9, but electrophoretic analysis revealed that calreticulin oligomerized instead of unfolding. Structural analyses showed that the single C-terminal α-helix was of major importance to the conformational stability of calreticulin.
Document Type: Review Article
Affiliations: Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark;
Publication date: 2005-10-01
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