The effect of protein relaxation on charge-charge interactions and dielectric constants of proteins

摘要: Abstract The effect of the reorganization protein polar groups on charge-charge interaction and corresponding effective dielectric constant (∈ eff ) is examined by semimicroscopic version Protein Dipole Langevin Dipoles (PDLD/S) method within framework Linear Response Approximation (LRA). This done evaluating interactions between ionized residues in reaction center Rhodobacter sphaeroides , while taking into account energy. It found that an explicit consideration relaxation leads to a significant increase ∈ models do not take this force one use large value for so-called "protein constant," p Poisson-Boltzmann model or PDLD/S model. An additional expected from changes degree water penetration. finding provides further support idea (or represents contributions are considered explicitly. present study also systematic illustration nature supporting our previously reported view correspond "dielectric even interiors. pointed out ionizable proteins very different constant, ∈′ determines free energy ion pairs (∈′ reflects preoriented dipoles). Finally, problems associated with search general discussed. clarified reproduces equal upon formation individual charges. fundamental inconsistencies attempts cast microscopic concepts macroscopic Thus should either small charge-dipole consider microscopically.