Equivalence of certain models in protein ligand equilibria and the possibility of distinguishing between them.

[1]  M E Magar,et al.  Analysis of protein ligand equilibria. , 1971, Journal of theoretical biology.

[2]  M. E. Magar,et al.  Molecular weight distribution functions and virial coefficients from sedimentation equilibrium data. , 1970, Journal of theoretical biology.

[3]  E. Whitehead.  Remarks on the kinetics of enzymes with interacting effector molecules. Tests of a configurational hypothesis in a quasi-equilibrium model. , 1970, Biochemistry.

[4]  J E Fletcher,et al.  A procedure for computer analysis of data from macromolecule-ligand binding studies. , 1968, Computers and biomedical research, an international journal.

[5]  Carl Frieden.  Treatment of enzyme kinetic data. II. The multisite case: comparison of allosteric models and a possible new mechanism. , 1967, The Journal of biological chemistry.

[6]  D. Koshland,et al.  Models for cooperative effects in proteins containing subunits. Effects of two interacting ligands. , 1967, The Journal of biological chemistry.

[7]  J P Changeux,et al.  On the nature of allosteric transitions: implications of non-exclusive ligand binding. , 1966, Journal of molecular biology.

[8]  J. Changeux,et al.  ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.

[9]  R. Steiner.  Reversible association processes of globular proteins. IV. Fluorescence methods in studying protein interactions. , 1953, Archives of biochemistry and biophysics.

[10]  G. Scatchard,et al.  THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS , 1949 .