Ornithine carbamoyltransferase unfolding states in the presence of urea and guanidine hydrochloride.

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.

authors

Barreca D,Laganà G,Ficarra S,Tellone E,Leuzzi U,Galtieri A,Bellocco E

doi

10.1007/s12010-013-0580-9

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

854-66

issue

2

eissn

0273-2289

issn

1559-0291

journal_volume

172

pub_type

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