- negative cooperativity
- cooperativity in which the dissociation constant for each successive ligand bound is higher than for the one preceding it, so that the binding affinity is successively decreased.
Medical dictionary. 2011.
negative cooperativity
Look at other dictionaries:
Cooperativity — is a phenomenon displayed by enzymes or receptors that have multiple binding sites where the affinity of the binding sites for a ligand is increased, positive cooperativity, or decreased, negative cooperativity, upon the binding of a ligand to a… … Wikipedia
cooperativity — Phenomenon displayed by enzymes or receptors that have multiple binding sites. Binding of one ligand alters the affinity of the other site(s). Both positive and negative cooperativity are known; positive cooperativity gives rise to a sigmoidal… … Dictionary of molecular biology
cooperativity — /koh op euhr euh tiv i tee/, n. Biochem. the increase or decrease in the rate of interaction between a reactant and a protein as the reactant concentration increases. Also, co operativity. [COOPERATIVE + ITY] * * * ▪ enzymology in… … Universalium
cooperativity — A property of certain proteins (often enzymes) in which the binding curves or saturation curves or, in the case of enzymes, a plot of initial rates as a function of initial substrate concentration, are nonhyperbolic; suggests that the binding of… … Medical dictionary
protein — proteinaceous /proh tee nay sheuhs, tee i nay /, proteinic, proteinous, adj. /proh teen, tee in/, n. 1. Biochem. any of numerous, highly varied organic molecules constituting a large portion of the mass of every life form and necessary in the… … Universalium
Enzyme kinetics — is the study of the chemical reactions that are catalysed by enzymes, with a focus on their reaction rates. The study of an enzyme s kinetics reveals the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled,… … Wikipedia
Cooperative binding — In biochemistry, a macromolecule exhibits cooperative binding if its affinity for its ligand changes with the amount of ligand already bound. Cooperative binding is a special case of allostery. Cooperative binding requires that the macromolecule… … Wikipedia
Hill equation — The Hill equation is an equation used in biochemical characterization, which should not be confused with the Hill differential equation that is also sometimes referred to as simply the Hill equation or Hill s equation .In biochemistry, the… … Wikipedia
Glutamate dehydrogenase 1 — GLUD1 (Glutamate dehydrogenase 1) is a mitochondrial matrix enzyme, with a key role in the nitrogen and glutamate (Glu) metabolism and the energy homeostasis. GLUD1 is expressed at high levels in liver, brain, pancreas and kidney, but not in… … Wikipedia
Propionyl-CoA carboxylase — PCCA redirects here. For other uses, see PCCA (disambiguation). Propionyl CoA carboxylase Identifiers EC number 6.4.1.3 CAS number … Wikipedia
