Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Renatured (Commentary)

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 2 of 2
download as CSV
download all results as CSV
EC Number Renatured (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.18.1.2equilibrium unfolding of enzyme by urea is a cooperative process where no stabilization of any partially folded intermediate of protein is observed. In comparison, unfolding by guanidinium chloride proceeds through intermediates that are stabilized by interaction of protein with guanidinium chloride. At a guanidinium chloride concentration of 0.8 M, stabilization of apoprotein is observed, resulting from direct binding of the guanidinium cation to protein 673522
Display the word mapDisplay the reaction diagram Show all sequences 1.18.1.2on thermal treatment, native enzyme undergoes partial denaturation with unfolding of only the FAD-binding domain and release of the protein-bound flavin. Thermal treatment in presence of either 150 mM NaCl or KCl or 0.01 mM MgCl2 or CaCl2 or pH of 6.0, results in a highly cooperative and complete thermal unfolding of the protein. Cations and pH 6.0 destabilize only the heat-stable NADP-binding domain 677007
Results 1 - 2 of 2
download as CSV
download all results as CSV