Proteins in the electric field near the surface of mica.

We elucidate the nature of the electric field produced by a model mica surface and show that above some 0.4 nm it is nearly uniform and of order 12 V/nm. The presence of ions in the solvent above the surface, up to the concentration of about 300 mM, does not modify the nature of the field much. We study the conformational changes of a small protein, the tryptophan cage, as induced by (a) uniform electric field and (b) the electric field near mica. We use all-atom molecular dynamics simulations and provide evidence for the existence of unfolded and deformed conformations in each of these cases. The two behaviors are characterized by distinct properties of the radius of gyration and of the distortion parameter that distinguishes between elongated and globular shapes. The overall geometry of the conformations shifts with the strengths of the uniform field in a manner that depends on the nature of the simulation box--whether it is bounded by neutral walls or not--and on the ionic concentration. Near the mica surface, on the other hand, the fraction of unfolded conformations is close to 1/6 at the ionic strength of 350 mM compared to 1/2 at 20 mM. When the electric charge on the mica is fully neutralized by bringing more ions of the opposite charge then unfolded conformations stay unfolded but an evolution from the native state does not lead to any unfolding.