Allostery

Molecular Symmetry and Metastable States of Enzymes Exhibiting Half-of-the-Sites Reactivity. Herzfeld J, Ichiye T and Jung D. Biochemistry 20, 4936-4941 (1981).

Kinetics of Cooperative Ligand Binding in Proteins: The Effects of Organic Phosphates on Hemoglobin Oxygenation. Bansil R, Herzfeld J and Stanley HE. J Mol Biol 103, 89-126 (1976).

Analysis of the Allosteric Basis for Positive and Negative Cooperativity and Half-of-the-Sites Reactivity in Yeast and Rabbit-Muscle Glyceraldehyde 3-Phosphate Dehydrogenase. Herzfeld J and Schlesinger PA. J Mol Biol 97, 483-517 (1975).

Hemoglobin Kinetics and the Effect of Organic Phosphates. Bansil R, Herzfeld J and Stanley HE. Science 186, 929-932 (1974).

A General Approach to Cooperativity and Its Application to the Oxygen Equilibrium of Hemoglobin and Its Effectors. Herzfeld J and Stanley HE. J Mol Biol 82, 231-265 (1974).

A General Model of Cooperativity and Its Application to DPG Inhibition of Hemoglobin Oxygenation. Herzfeld J and Stanley HE. Biochem Biophys Res Comm 48, 307-313 (1972).