The self-association of adenosine-5'-triphosphate studied by circular dichroism at low ionic strengths.
The self-association of adenosine-5'-triphosphate (ATP) was studied as a function of pH, additional counterions, concentration and temperature. Circular dichroism measurements were employed as a measure of the base-stacking. The self-association of ATP is pH dependent with the protonation of the adenine ring helping stabilize the association. Highly charged counterions alter this aggregation. At pH 2.8 and 20 degrees C, a dimerization constant of 88 M-1 is obtained, while an isodesmic model leads to an equilibrium constant of 158 M-1. With increasing pH, the association constants decrease. At pH 2.8 there is a very strong temperature dependence of the CD amplitude. These results indicate the existence of additional electrostatic stabilization for the stacking of the adenine rings. At acidic pHs, models are proposed to explain this high degree of stability and a calculation of the approximate electrostatic contribution to the aggregation shows it to be of the proper magnitude.
D000255:Adenosine Triphosphate; D001665:Binding Sites; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D008433:Mathematics; D008958:Models, Molecular; D008968:Molecular Conformation; D009994:Osmolar Concentration; D013056:Spectrophotometry, Ultraviolet
D000255:Adenosine Triphosphate