Effects of As(III) binding on [beta]-hairpin structure

Effects of arsenic binding on [Beta]-hairpin are studied by introducing pairs of cysteines into a model monomeric [Beta]-hairpin to yield a family of peptides. Results reveal that arsenic binding could both favor and disfavor helical and [Beta]-hairpin structures depending on the placement of cysteine residues and the plasticity of the secondary structural elements to insertion of a monoalkylated As(III) derivative.