[Intraglobular electrostatic field of an enzyme. Calculation of the dissociation constant of a protein ionogenic group. Dissociation of Asp-102 chymotrypsin].
Factors determining the change of dissociation constants of ionogenic groups upon their transfer from water into a protein globule are considered. The change of the short-range interaction is simulated with the aid of two model solvents: dimethylformamide (DMF) and formamide (FA). The change of Bornian solvation energy is calculated taking into account the interaction of ions situated inside a protein globule with the surrounding electrolyte solution. The change of ion energy due to the intraglobular electric field preexisting in the enzyme molecule is calculated. Each of the factors listed above gives a large contribution into the ion energy in the case of Asp-102 these contributions compensate each other to a great extent.
D001224:Aspartic Acid / Q000378:metabolism*; D001665:Binding Sites; D002918:Chymotrypsin / Q000378:metabolism*; D004560:Electricity; D004579:Electron Transport; D006860:Hydrogen Bonding; D007700:Kinetics; D008954:Models, Biological; D012997:Solvents
D012997:Solvents; D001224:Aspartic Acid; D002918:Chymotrypsin
Vnutriglobuliarnoe élektrostaticheskoe pole fermenta. III. Raschet konstanty dissotsiatsii ionogennoĭ gruppy v belke. Dissotsiatsiia Asp-102 alpha-khimotripsina.