Urea and guanidinium chloride denature Protein L in different ways in molecular dynamics simulations
Articolo
Data di Pubblicazione:
2008
Citazione:
Urea and guanidinium chloride denature Protein L in different ways in molecular dynamics simulations / C. Camilloni, A. Guerini Rocco, I. Eberini, E. Gianazza, R.A. Broglia, G. Tiana. - In: BIOPHYSICAL JOURNAL. - ISSN 0006-3495. - 94:12(2008), pp. 4654-4661.
Abstract:
In performing protein-denaturation experiments, it is common to employ different kinds of denaturants interchangeably. Wemake use of molecular dynamics simulations of Protein L in water, in urea, and in guanidinium chloride (GdmCl) to ascertain if there are any structural differences in the associated unfolding processes. The simulation of proteins in solutions of GdmCl is complicated by the large number of charges involved, making it difficult to set up a realistic force field. Furthermore, at high concentrations of this denaturant, the motion of the solvent slows considerably. The simulations show that the unfolding mechanism depends on the denaturing agent: in urea the β-sheet is destabilized first, whereas in GdmCl, it is the α-helix. Moreover, whereas urea interacts with the protein accumulating in the first solvation shell, GdmCl displays a longer-range electrostatic effect that does not perturb the structure of the solvent close to the protein.
Tipologia IRIS:
01 - Articolo su periodico
Elenco autori:
C. Camilloni, A. Guerini Rocco, I. Eberini, E. Gianazza, R.A. Broglia, G. Tiana
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