Protein Variants | Comment | Organism |
---|---|---|
Y74C | urea unfolding profiles of Y74Cox in urea solution obtained by fluorescence and circular dichroism approximate a two-state transition and do not show the presence of stable intermediates over a wide range of denaturant concentrations. In wild-type enzyme the unfolding results in gradual change in spectroscopic properties. The unfolding transition midpoit is 3.5 M for Y74Cox and 5.5 M for the wild-type enzyme | Plasmodium falciparum |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
27000 | - |
x * 27000, SDS-PAGE | Plasmodium falciparum |
27832 | - |
x * 27832, electrospray mass spectrometry | Plasmodium falciparum |
Organic Solvent | Comment | Organism |
---|---|---|
guanidine-HCl | 2.4 M, the unfolding transition is complete | Plasmodium falciparum |
urea | the unfolding transition midpoit is 3.5 M for Y74Cox and 5.5 M for the wild-type enzyme. The dimeric wild-type enzyme retains considerable secondary, tertiary, and quarternary structure even in 8 M urea. Urea unfolding profiles of Y74Cox in urea solution obtained by fluorescence and circular dichroism approximate a two-state transition and do not show the presence of stable intermediates over a wide range of denaturant concentrations. In wild-type enzyme the unfolding results in gradual change in spectroscopic properties | Plasmodium falciparum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
wild-type and mutant enzyme Y74C | Plasmodium falciparum |
Subunits | Comment | Organism |
---|---|---|
? | x * 27000, SDS-PAGE | Plasmodium falciparum |
? | x * 27832, electrospray mass spectrometry | Plasmodium falciparum |