Conformational Stability of Calreticulin

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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.

Keywords: calreticulin; conformation; heat shock protein; oligomerization; stability

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866054696082

Affiliations: Department of Research and Development, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark;

Publication date: October 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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