  Recent experiments have identified peptides with adhesion affinity for GaAs
and Si surfaces. Here we use all-atom Monte Carlo (MC) simulations with
implicit solvent to investigate the behavior in aqueous solution of four such
peptides, all with 12 residues. At room temperature, we find that all the four
peptides are largely unstructured, which is consistent with experimental data.
At the same time, we find that one of the peptides is structurally different
and more flexible, compared to the others. This finding points at structural
differences as a possible explanation for differences in adhesion properties
between these peptides. By also analyzing designed mutants of two of the
peptides, an experimental test of this hypothesis is proposed.
