The Interactive Binding of Two Ligands by an Allosteric Protein
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1977.tb11721.x/fullpdf
Reference17 articles.
1. On the nature of allosteric transitions: A plausible model
2. Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*
3. Remarks on the kinetics of enzymes with interacting effector molecules. Tests of a configurational hypothesis in a quasi-equilibrium model
4. The regulation of enzyme activity and allosteric transition
5. The analysis of the binding of two ligands by an allosteric protein
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1. Quantitative aspects of the development of a hydrophobic binding site on calmodulin by calcium binding;Biopolymers;1984-06
2. Site-site interactions in glycogen phosphorylase b probed by ligands specific for each site;Biochemistry;1983-09-13
3. Properties of the complexes formed by 1-anilinonaphthalene-8-sulfonate with phosphorylase kinase and calmodulin;Biopolymers;1982-07
4. A kinetic analysis of the distinct regulatory sites on rabbit muscle pyruvate kinase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1982-04
5. Structural changes induced in glycogen phosphorylase by the binding of glucose and caffeine;Biochimica et Biophysica Acta (BBA) - Enzymology;1980-02
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