Given the potential adaptive benefit of cooperative regulation, it makes sense to ask, when will cooperative binding between a pair of transcription factors be able to invade a population that lacks such cooperativity?
All these results show that, given the binding affinities at equilibrium and the overall concentrations of the different components, mutual information quantifies for which protein concentrations the systems' cooperativity, or more specific its coordination, is optimal.
U2B″ binds U2A′ with nanomolar affinity, and the SLIV/U2B″/U2A′ ternary complex is characterized by a large cooperativity (linkage) parameter.
The large number of additional, lateral binding sites sometimes creates large cooperativity effects that enable filaments to bind with extreme affinity to their partner, even if the individual binding energies, per subunit, are rather small.
For example, the critical concentration becomes a function of two variables and this may result in very large cooperativity effects.
Give the Caped Crusader a large cape.
This phenomenon enables initial ligation of MLCK at the C-terminal domain of CaM and induces a population shift among the substates accessible to the N-terminal domain, thus giving rise to the cooperativity associated with binding.
Each TF pair is given a cooperativity score by our method.
Cooperative binding was observed, but all fluorinated acids gave a similar cooperativity parameter, and it was found that both the overall constant as well as the cooperative binding process, increases with the molecular weight of the polymer.
Thermodynamics of MT-DADMe-ImmA binding also gave negative cooperativity, where the first site had different enthalpic and entropic properties than the second site.
