The application of calculations of the electrostatic field of proteins in the choice of enzymes for microcapsulation
"Математика. Компьютер. Образование". Cб. трудов XII международной конференции. Под общей редакцией Г.Ю. Ризниченко Ижевск: Научно-издательский центр "Регулярная и хаотическая динамика", 2005. Vol. 3, 344pp. Pp. 923-933.
In the development of enzyme polyelectrolyte microreactors, some properties of enzymes, e. g., the isoelectric point of the protein pI, i. e., the value of its full charge Q, should be taken into account. However, of particular importance is exact knowledge of the distribution of the electrostatic potential on the surface of the protein. This paper is devoted to the calculation of the distribution of the electrostatic potential of some proteins with consideration of the local microenvironment for every charged amino acid residue and accordingly a change in the рКа value. The distribution of the electrostatic potential of ribonuclease A and lysozyme was calculated at different рН values 4,5, 6, 7 and 8, using both standard рКа values and рКа values corrected for local microenvironment for every titrated aminoacid residue of the protein. A comparison of these calculations showed that taking the microenvironment of amino acid residue into account changes the distribution of the electrostatic potential of enzymes in the limited рН range (3–5). The areas of regions with the corresponding distribution of the electrostatic potential on the protein surface that are capable of binding to the polyelectrolyte were calculated.The analysis of the distribution of the electrostatic potential in the рН range 5–8 of these proteins showed that the correction for the change in the рКа values does not appreciably affect the distribution of the electrostatic potential and that it can be neglected when constructing permolecular complexes.