Journal article
Conformational stability of calreticulin
The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (T-m) 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 a-helix was of major importance to the conformational stability of calreticulin.
Language: | English |
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Year: | 2005 |
Pages: | 687-693 |
ISSN: | 18755305 and 09298665 |
Types: | Journal article |
DOI: | 10.2174/0929866054696082 |
ORCIDs: | 0000-0001-9864-2287 |