Abstract
As an experimental analog for the assembly of alfalfa mosaic virus (AIMV), the association of coat protein subunits into empty capsids in the presence of ATP has been studied. It is found by equilibrium dialysis that the binding of ligands such as ATP to the coat protein is dependent on the polymerization state of the protein. The effect of ATP on the extent of polymerization is demonstrated by sedimentation analysis of reaction mixtures with different amounts of ATP. The experimental results are interpreted with a model for allosteric regulation of protein polymerization, put forward by Oosawa, F. and Higashi, S. ((1967) Prog. Theor. Biol. 1, 79–164). Essential in their theory is the assumption that the protein can adopt at least two different conformations, each with a different binding affinity for ligands. The model has been adapted to the polymerization and binding characteristics of the AIMV protein. It is demonstrated that the existence of different conformations of the protein is a prerequisite to explain the experimental data.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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