Abstract
THE tertiary structure of an isolated polypeptide chain may differ from its most stable conformation as a component of an oligomer. The assembly of free subunits into an oligomeric structure may therefore involve a relatively unstable oligomeric intermediate state in which the conformation of the subunits corresponds to that of the free polypeptide chains. Such a metastable intermediate state may be separated from the stable oligomer by a substantial energy barrier, and the marked temperature dependence of subunit association reactions has indeed been attributed to the existence of a “conformational transition state”1.
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ALPERS, J., PAULUS, H. Biological sciences: Allosteric Preconditioning: Role of Allosteric Ligands in Promoting the Maturation of Enzymes. Nature 233, 478–480 (1971). https://doi.org/10.1038/233478a0
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DOI: https://doi.org/10.1038/233478a0
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