Protein stability; optimization of electrostatic contributions by partially neutralizing surface ionic charges.
'Partial Charge-Neutralization Method' is developed to study influence of the relative amount of positive and negative charges in proteins on their structural stability. A given number of either positively or negatively charged groups are neutralized in all of their possible combinations to generate a whole set of distinct species. The Coulomb energy of each species is calculated by numerically solving the Poisson-Boltzmann equation for aqueous solutions. Partial neutralization of lysine residues of tuna cytochrome c in aqueous solution at neutral pH with the Debye-Hückel screening parameter kappa = 1 nm-1 reproduces qualitatively well the destabilization of acetylated cytochrome c observed in physicochemical measurements at pH 7. The stabilization of its molten globule state at pH 2 is also studied with the present method. It is shown that the electrostatic contribution to the structural stability of natural proteins can be optimized by changing the difference in number of their positive and negative charges.
Miki
Y
Y
Department of Bioengineering, Nagaoka University of Technology, Niigata, Japan.
Kakuyama
K
K
Soda
K
K
D003574:Cytochrome c Group / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007477:Ions; D008239:Lysine / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D055672:Static Electricity; D013816:Thermodynamics; D014452:Ubiquitins / Q000737:chemistry
D003574:Cytochrome c Group; D007477:Ions; D011506:Proteins; D014452:Ubiquitins; D008239:Lysine