Protein is an amphoteric polyelectrolyte with a globular and fairly rigid structure. Electrostatic effect has been found to take part in stabilizing this compact conformation. In this regard, we analyzed statistically the spatial distribution of tonic charges and partial atomic charges in 26 proteins. Local compensation between the positive and negative charges is found to be a general characteristic in globular proteins, which conducts the protein structure and its biochemical functions. This plus-minus charge compensation principle seems to govern in general the intra- and infer-molecular electrostatic interactions in biological macro-molecules including proteins, nucleic acids, and membrane components.
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Wada et al. (1985) studied this question.
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