Allostery in very large molecular assemblies
| Autor: | K. E. Van Holde, Karen I. Miller, Erin van Olden |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
genetic structures
Macromolecular Substances Stereochemistry medicine.medical_treatment Allosteric regulation Biophysics Cooperativity Biochemistry Allosteric Regulation medicine Animals Protein Structure Quaternary biology Chemistry Organic Chemistry Cooperative binding Hemocyanin Oxygen Allosteric enzyme Mollusca Chemical physics Hemocyanins biology.protein Protein quaternary structure Dimerization Oxygen binding Macromolecule |
| Zdroj: | Biophysical Chemistry. 86:165-172 |
| ISSN: | 0301-4622 |
| Popis: | In contrast to small allosteric systems (like hemoglobin) those containing very large numbers ( n ) of binding sites never exhibit cooperativity (as measured by the Hill coefficient, n H ) even approaching the potential limit, n . The reason for this appears to be that in such macromolecules the cooperative unit always represents some sub-structure of the entire structure. On the other hand, it is frequently observed that such sub-structures, when isolated, do not exhibit cooperativity at all. This paper describes studies of some molluscan hemocyanins that explore this apparent anomoly. It is concluded that it is the higher order structure of the molecule that provides a framework within which the sub-structures may exhibit their allosteric behavior. |
| Databáze: | OpenAIRE |
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