The interaction of guanidinium ions with a model peptide.

ABSTRACT: In addition to promoting unfolded protein states, the denaturants urea and guanidinium (Gdm(+)) accumulate at the surface of folded proteins at subdenaturing concentrations, a phenomenon that correlates with their denaturant activities. The enhanced accumulation of Gdm(+) relative to urea indicates different binding modes, or additional binding sites, for Gdm(+), and we recently proposed potential binding modes to protein functional groups for Gdm(+) based on the determination of the weak hydration properties of this complex cation. Here we describe molecular dynamics simulations of a model helical peptide, melittin, in a 3 M solution of GdmCl, to identify potential interactions with amino-acid side chains in a nondenatured polypeptide surface. The simulations indicate that Gdm(+) can inte

SUBMITTER: Mason PE 

PROVIDER: S-EPMC1914420 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature