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Urea and guanidinium chloride denature protein L in different ways in molecular dynamics simulations.


ABSTRACT: In performing protein-denaturation experiments, it is common to employ different kinds of denaturants interchangeably. We make 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 beta-sheet is destabilized first, whereas in GdmCl, it is the alpha-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.

SUBMITTER: Camilloni C 

PROVIDER: S-EPMC2397339 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Urea and guanidinium chloride denature protein L in different ways in molecular dynamics simulations.

Camilloni C C   Rocco A Guerini AG   Eberini I I   Gianazza E E   Broglia R A RA   Tiana G G  

Biophysical journal 20080313 12


In performing protein-denaturation experiments, it is common to employ different kinds of denaturants interchangeably. We make 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  ...[more]

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