Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
unfolding in 6 M guanidine hydrochloride for different periods of time. Reactivation of equilibrium-unfolded mAAT is sigmoidal, reactivation of the short term unfolded protein displays a double exponential behavior consistent with the presence of fast and slow refolding species. The presence of coenzyme does not perturb the kinetics or pathway of refolding. Covalently attached PLP slows down the interconversion between fast and slow folding populations of unfolded states. Additional structural rearrangements occurring both in the unfolded state and in populations of folding intermediates along the folding pathway | Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Rattus norvegicus |