Ornithine Carbamoyltransferase Unfolding States in the Presence of Urea and Guanidine Hydrochloride |
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Authors: | D. Barreca G. Laganà S. Ficarra E. Tellone U. Leuzzi A. Galtieri E. Bellocco |
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Affiliation: | 1. Dipartimento di Scienze Chimiche, Università di Messina, Viale F. Stagno d’Alcontres 31, 98166, Messina, Italy
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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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