In both nature and physicochemical treatment, virus end depends on electrostatic interplays. Suggesting an exact method of predicting virion isoelectric point (IEP) would assist to comprehend and predict virus end. To predict IEP, an easy method evaluates the pH at which the total of charges from ionizable amino acids in capsid proteins reaches zero. Founded on capsid charges, however, predicted IEPs usually diverge by some pH units from experimentally measured IEPs. Such disparity between experimental and predicted IEP was ascribed to the electrostatic neutralization of predictable polynucleotide- binding regions (PBRs) of the capsid interior. In the first part of this work, models assuming the 1) impact of the viral polynucleotide on the surface charge, or 2) contribution of only exterior residues to surface charge are discussed. Such models are relevant to non-enveloped viruses only, and an identical model for enveloped viruses remains difficult by the deficiency of information on enveloped virus IEP and uncertainties concerning the effect of the phospholipid envelope on charge and ion gradients. It is difficult now that modeling IEPs for viruses could be employed in assessing the needed electric field application during electrocoagulation (EC) process. Parameters such as pH and aqueous matrix greatly influence IEPs and EC.
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