Literature DB >> 8571449

Cooperativity: over the Hill.

S Forsén1, S Linse.   

Abstract

Cooperativity, the ability of ligand binding at one site on a macromolecule to influence ligand binding at a different site on the same macromolecule, is a fascinating biological property that is often poorly explained in textbooks. The Hill coefficient is commonly used in biophysical studies of cooperative systems although it is not a quantitative measure of cooperativity. The free energy of interaction between binding sites (delta delta G) is a more stringent definition of cooperativity and provides a direct quantitative measure of how the binding of ligand at one site affects the ligand affinity of another site.

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Year:  1995        PMID: 8571449     DOI: 10.1016/s0968-0004(00)89115-x

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  20 in total

1.  Identification of a tertiary interaction important for cooperative ligand binding by the glycine riboswitch.

Authors:  Thanh V Erion; Scott A Strobel
Journal:  RNA       Date:  2010-11-23       Impact factor: 4.942

2.  Chemical basis of glycine riboswitch cooperativity.

Authors:  Miyun Kwon; Scott A Strobel
Journal:  RNA       Date:  2007-11-27       Impact factor: 4.942

3.  Reassessing a sparse energetic network within a single protein domain.

Authors:  Celestine N Chi; Lisa Elfström; Yao Shi; Tord Snäll; Ake Engström; Per Jemth
Journal:  Proc Natl Acad Sci U S A       Date:  2008-03-13       Impact factor: 11.205

4.  Measuring positive cooperativity using the direct ESI-MS assay. Cholera toxin B subunit homopentamer binding to GM1 pentasaccharide.

Authors:  Hong Lin; Elena N Kitova; John S Klassen
Journal:  J Am Soc Mass Spectrom       Date:  2014-01       Impact factor: 3.109

5.  Electrostatic coupling to pH-titrating sites as a source of cooperativity in protein-ligand binding.

Authors:  V Spassov; D Bashford
Journal:  Protein Sci       Date:  1998-09       Impact factor: 6.725

6.  Cystathionine β-synthase (CBS) domains confer multiple forms of Mg2+-dependent cooperativity to family II pyrophosphatases.

Authors:  Anu Salminen; Viktor A Anashkin; Matti Lahti; Heidi K Tuominen; Reijo Lahti; Alexander A Baykov
Journal:  J Biol Chem       Date:  2014-07-01       Impact factor: 5.157

7.  On Hill coefficients and subunit interaction energies.

Authors:  Hagai Abeliovich
Journal:  J Math Biol       Date:  2016-04-01       Impact factor: 2.259

8.  Effects of Ca2+, Mg2+, and myristoylation on guanylyl cyclase activating protein 1 structure and stability.

Authors:  Sunghyuk Lim; Igor Peshenko; Alexander Dizhoor; James B Ames
Journal:  Biochemistry       Date:  2009-02-10       Impact factor: 3.162

9.  Dissecting cooperative calmodulin binding to CaM kinase II: a detailed stochastic model.

Authors:  Michael J Byrne; John A Putkey; M Neal Waxham; Yoshihisa Kubota
Journal:  J Comput Neurosci       Date:  2009-07-17       Impact factor: 1.621

10.  The Role of Magnesium, Pyrophosphate, and Their Complexes as Substrates and Activators of the Vacuolar H+-Pumping Inorganic Pyrophosphatase (Studies Using Ligand Protection from Covalent Inhibitors).

Authors:  R. Gordon-Weeks; S. H. Steele; R. A. Leigh
Journal:  Plant Physiol       Date:  1996-05       Impact factor: 8.340

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