Abstract
Ornithine carbamoyltransferase folding/unfolding is a complex and not completely understood process. Our experimental results suggest that ornithine carbamoyltransferase interacts in a completely different way with urea and guanidine hydrochloride. In fact, we noticed that, increasing concentration from 0.0 to 8.0 M of the two additives, the enzyme follows a simple one-step transition mechanism in the presence of guanidine hydrochloride, with two macroscopic states (the native and the denatured one) significantly populated, whereas in the presence of urea a lot of different protein states can be detected and analyzed. Circular dichroism and UV-visible spectroscopy reveal a similar mechanism of perturbation at high temperature, with opening of hydrophobic core and a significant loss in α-helix structure in the presence of guanidine hydrochloride that cannot be found in the presence of urea.
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Barreca, D., Laganà, G., Ficarra, S. et al. Ornithine Carbamoyltransferase Unfolding States in the Presence of Urea and Guanidine Hydrochloride. Appl Biochem Biotechnol 172, 854–866 (2014). https://doi.org/10.1007/s12010-013-0580-9
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DOI: https://doi.org/10.1007/s12010-013-0580-9