Cooperativity is a phenomenon in biology displayed by enzymes or receptors that have multiple binding sites.
When substrate bonds to the active site of one enzymatic subunit, the rest of the subunits are stimulated and become active.
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Cooperativity A property of many allosteric enzymes in which the binding of substrate to one active site favors the transition of all active sites from the T state to the R state, leading to an increase in enzyme activity.
Cooperativity is observed when two synapses are activated by weak stimuli incapable of inducing LTP when stimulated individually. But upon simultaneous weak stimulation, both synapses undergo LTP in a cooperative fashion.
This cooperativity is provided by mutually complementary segments in the two modules that bind to each other forming what is termed a "stem" region. Before actual PCR can take place, a branched primer is extended along the template.
For DNA binding proteins, cooperativity generally refers to the increased binding of a protein to a DNA site due to the prior binding of another protein nearby.
 See also: Protein, Enzyme, Trans, DNA, Proteins
  
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