Allowance for effects of electrostatic repulsion on protein dimerization.
A simple procedure for assessing the extent of electrostatic effects on protein dimerization is described and illustrated by application to published results on the ionic strength dependence of the dimerization constant for alpha-chymotrypsin at pH 4 (Aune, K.C., Goldsmith, L.C. and Timasheff, S.N. (1971) Biochemistry 10, 1617-1622). From the analysis it is concluded that the inverse dependence of alpha-chymotrypsin dimerization upon ionic strength is predominantly a general electrostatic effect, rather than a consequence of repulsion between two specific charged residues on the adjacent monomers comprising dimer.
Agapow
P M
PM
Department of Biochemistry, University of Queensland, St. Lucia, Australia.
Winzor
D J
DJ
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002918:Chymotrypsin; D004563:Electrochemistry; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D009994:Osmolar Concentration; D011506:Proteins; D013816:Thermodynamics
D046911:Macromolecular Substances; D011506:Proteins; D002918:Chymotrypsin