Characterization of alkaline transitions in ferricytochrome c using carbon-deuterium infrared probes.

ABSTRACT: The alkaline-induced structural transitions of ferricytochrome c have been studied intensively as a model for how changes in metal ligation contribute to protein function and folding. Previous studies have demonstrated that multiple non-native species accumulate with increasing pH. Here, we used a combination of experiments and simulations to provide a high-resolution view of the changes associated with increasing alkaline conditions. Alkaline-induced transitions were characterized under equilibrium conditions by following changes in the IR absorptions of carbon-deuterium chromophores incorporated at Leu68, Lys72, Lys73, Lys79, and Met80. The data suggest that at least four intermediates are formed as the pH is increased prior to complete unfolding of the protein. The first alkaline transi

SUBMITTER: Weinkam P 

PROVIDER: S-EPMC2853379 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature