The ionization of clusters. II. Pairwise isotropic interactions and individual site binding data.
Evaluation of the parameters describing the binding of protons to clusters of interacting sites requires some reasonable assumptions and procedures because it is impossible to observe an unperturbed site in its interacting environment. When the unperturbed sites are not identical, individual site binding data allow for the evaluation of the differences (or ratios) between the unperturbed (or intrinsic) binding constants but not their actual values (or the interaction energies). In this paper we extend our previous treatment of the ionization of clusters in order to generalize pairwise isotropic interactions and take into account the present availability of individual site binding data.
Saroff
H A
HA
Laboratory of Biochemical Pharmacology, National Institute of Arthritis, Bethesda, Maryland 20892.
D001665:Binding Sites; D004163:Diphosphoglyceric Acids / Q000378:metabolism; D005029:Ethylenediamines / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010710:Phosphates / Q000378:metabolism; D011522:Protons; D013816:Thermodynamics
D004163:Diphosphoglyceric Acids; D005029:Ethylenediamines; D010710:Phosphates; D011522:Protons