Abstract:
:Calreticulin is a soluble endoplasmic reticulum chaperone, which has a relatively low melting point due to its remarkable structure with a relatively high content of flexible structural elements. Using far ultraviolet circular dichroism (CD) spectroscopy and a fluorescent dye binding thermal shift assay, we have investigated the chemical and thermal stability of calreticulin. When the chemical stability of calreticulin was assessed, a midpoint for calreticulin unfolding was calculated to 3.0M urea using CD data at 222 nm. Using the fluorescent dye binding thermal shift assay, calreticulin was found to obtain a molten structure in urea concentrations between 1-1.5 M urea, and to unfold/aggregate at high and low pH values. The results demonstrated that the fluorescent dye binding assay could measure the thermal stability of calreticulin in aqueous buffers with results comparable to melting points obtained by other techniques.
journal_name
Protein Pept Lettjournal_title
Protein and peptide lettersauthors
Duus K,Larsen N,Tran TA,Güven E,Skov LK,Jespersgaard C,Gajhede M,Houen Gdoi
10.2174/0929866511320050009subject
Has Abstractpub_date
2013-05-01 00:00:00pages
562-8issue
5eissn
0929-8665issn
1875-5305pii
PPL-EPUB-20120914-1journal_volume
20pub_type
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journal_title:Protein and peptide letters
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