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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1988 Jan;85(2):449–452. doi: 10.1073/pnas.85.2.449

Binding capacity: cooperativity and buffering in biopolymers.

E Di Cera 1, S J Gill 1, J Wyman 1
PMCID: PMC279567  PMID: 3422436

Abstract

The group of linkage potentials resulting from the energy of a physicochemical system expressed per mol of a reference component, say a polyfunctional macromolecule, leads to the concept of binding capacity. This concept applies equally to both chemical and physical ligands and opens the way to consideration of higher-order linkage relationships. It provides a means of exploring the consequences of thermodynamic stability on generalized binding phenomena in biopolymers.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Dolman D., Gill S. J. Membrane-covered thin-layer optical cell for gas-reaction studies of hemoglobin. Anal Biochem. 1978 Jun 15;87(1):127–134. doi: 10.1016/0003-2697(78)90576-6. [DOI] [PubMed] [Google Scholar]
  2. Doyle M. L., Di Cera E., Robert C. H., Gill S. J. Carbon dioxide and oxygen linkage in human hemoglobin tetramers. J Mol Biol. 1987 Aug 20;196(4):927–934. doi: 10.1016/0022-2836(87)90414-1. [DOI] [PubMed] [Google Scholar]
  3. Gill S. J., Di Cera E., Doyle M. L., Bishop G. A., Robert C. H. Oxygen binding constants for human hemoglobin tetramers. Biochemistry. 1987 Jun 30;26(13):3995–4002. doi: 10.1021/bi00387a038. [DOI] [PubMed] [Google Scholar]
  4. Gill S. J., Richey B., Bishop G., Wyman J. Generalized binding phenomena in an allosteric macromolecule. Biophys Chem. 1985 Jan;21(1):1–14. doi: 10.1016/0301-4622(85)85001-8. [DOI] [PubMed] [Google Scholar]
  5. Privalov P. L. Stability of proteins: small globular proteins. Adv Protein Chem. 1979;33:167–241. doi: 10.1016/s0065-3233(08)60460-x. [DOI] [PubMed] [Google Scholar]
  6. Rollema H. S., de Bruin S. H., Janssen L. H., van Os G. A. The effect of potassium chloride on the Bohr effect of human hemoglobin. J Biol Chem. 1975 Feb 25;250(4):1333–1339. [PubMed] [Google Scholar]
  7. WYMAN J., Jr LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK. Adv Protein Chem. 1964;19:223–286. doi: 10.1016/s0065-3233(08)60190-4. [DOI] [PubMed] [Google Scholar]
  8. WYMAN J. THE BINDING POTENTIAL, A NEGLECTED LINKAGE CONCEPT. J Mol Biol. 1965 Mar;11:631–644. doi: 10.1016/s0022-2836(65)80017-1. [DOI] [PubMed] [Google Scholar]
  9. Wyman J. A group of thermodynamic potentials applicable to ligand binding by a polyfunctional macromolecule. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1464–1468. doi: 10.1073/pnas.72.4.1464. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Wyman J. Linkage graphs: a study in the thermodynamics of macromolecules. Q Rev Biophys. 1984 Nov;17(4):453–488. doi: 10.1017/s0033583500004881. [DOI] [PubMed] [Google Scholar]
  11. Wyman J. Regulation in macromolecules as illustrated by haemoglobin. Q Rev Biophys. 1968 May;1(1):35–80. doi: 10.1017/s0033583500000457. [DOI] [PubMed] [Google Scholar]

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