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.
journal_name
Appl Biochem Biotechnoljournal_title
Applied biochemistry and biotechnologyauthors
Barreca D,Laganà G,Ficarra S,Tellone E,Leuzzi U,Galtieri A,Bellocco Edoi
10.1007/s12010-013-0580-9subject
Has Abstractpub_date
2014-01-01 00:00:00pages
854-66issue
2eissn
0273-2289issn
1559-0291journal_volume
172pub_type
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