cooperativityn.

Brit.

/kəʊˌɒp(ə)rəˈtɪvᵻti/, U.S.

/koʊˌɑp(ə)rəˈtɪvᵻdi/

Origin: Formed within English, by derivation. Etymons: cooperative adj., -ity suffix.

Etymology: < cooperative adj. + -ity suffix.

Biochemistry.

An effect or property whereby the binding of a ligand to one site in a protein or other macromolecule alters the tendency of other sites in the molecule to bind further ligands; (also) the strength or extent of such an effect.The effect may increase the affinity of sites for further ligands ( positive cooperativity) or decrease it ( negative cooperativity). The binding of oxygen to haemoglobin, for example, displays positive cooperativity.

ΚΠ

1965 J. Monod et al. in Jrnl. Molecular Biol. 12 91 In such graphs the co-operative homotropic effect of the ligand, predicted by the symmetry properties of the model, is expressed by the curvature of the lower part of the curves. The graphs illustrate the fact that the ‘co-operativity’ of the ligand depends upon the values of L and c.

1968 Biochemistry 7 4011/2 The results indicate a ‘negative cooperativity’ in which the binding of each molecule of DPN [= diphosphopyridine nucleotide] makes it more difficult for the next molecule to bind.

1975 I. H. Segel Enzyme Kinetics vii. 377 We have considered allosteric enzymes that exhibit positive cooperativity with respect to substrate binding.

1979 Nature 9 Aug. 448/3 These structural changes seem to bear obvious relationships to the known homotropic and heterotropic cooperativities of the enzyme.

1997 G. S. Helfman et al. Diversity of Fishes v. 58/1 The four subunits of the hemoglobin molecule exhibit subunit cooperativity and help the molecule load up with oxygen quickly once the first molecule is bound.

2014 T. A. Waigh Physics Living Processes v. 97 Biological helices normally demonstrate a high degree of cooperativity.

This is a new entry (OED Third Edition, September 2016; most recently modified version published online March 2022).

单词	cooperativity
释义	cooperativityn. Brit. /kəʊˌɒp(ə)rəˈtɪvᵻti/, U.S. /koʊˌɑp(ə)rəˈtɪvᵻdi/ Origin: Formed within English, by derivation. Etymons: cooperative adj., -ity suffix. Etymology: < cooperative adj. + -ity suffix. Biochemistry. An effect or property whereby the binding of a ligand to one site in a protein or other macromolecule alters the tendency of other sites in the molecule to bind further ligands; (also) the strength or extent of such an effect.The effect may increase the affinity of sites for further ligands ( positive cooperativity) or decrease it ( negative cooperativity). The binding of oxygen to haemoglobin, for example, displays positive cooperativity. ΚΠ 1965 J. Monod et al. in Jrnl. Molecular Biol. 12 91 In such graphs the co-operative homotropic effect of the ligand, predicted by the symmetry properties of the model, is expressed by the curvature of the lower part of the curves. The graphs illustrate the fact that the ‘co-operativity’ of the ligand depends upon the values of L and c. 1968 Biochemistry 7 4011/2 The results indicate a ‘negative cooperativity’ in which the binding of each molecule of DPN [= diphosphopyridine nucleotide] makes it more difficult for the next molecule to bind. 1975 I. H. Segel Enzyme Kinetics vii. 377 We have considered allosteric enzymes that exhibit positive cooperativity with respect to substrate binding. 1979 Nature 9 Aug. 448/3 These structural changes seem to bear obvious relationships to the known homotropic and heterotropic cooperativities of the enzyme. 1997 G. S. Helfman et al. Diversity of Fishes v. 58/1 The four subunits of the hemoglobin molecule exhibit subunit cooperativity and help the molecule load up with oxygen quickly once the first molecule is bound. 2014 T. A. Waigh Physics Living Processes v. 97 Biological helices normally demonstrate a high degree of cooperativity. This is a new entry (OED Third Edition, September 2016; most recently modified version published online March 2022). < n.1965
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