Sentence examples for control the affinity from inspiring English sources

While the acidic tails of tubulin control the affinity of MCAK for microtubules, they are not necessary for the displacement of the MCAK CT domain from the motor.

Since NFATc1/alphaA suppresses the RNA synthesis of secreted IgM and Blimp-1 but enhances Bcl-6 and Bach-2 RNA levels, NFATc1/alphaA appears to control the affinity maturation of Ig genes in germinal center (GC) B cells.

For additional quality control, the affinities for binding of the BMP-2 and GDF-5 proteins to BMPR-IA and other type I and type II receptors were determined by surface plasmon resonance as previously described and compared to published data [ 17].

Considering that a single mutation of one aromatic amino acid lowers the processivity and increases hydrolytic activity in ChiA as demonstrated in the former biochemical study22, the balance between velocity and processivity is 'fine-tuned' by controlling the affinity with the substrates15.

Additionally, we found that syndecan-1 augmented cell adhesion to collagen by controlling the affinity state of the α2β1 integrin.

These data indicate that syndecan-1 modulates cell adhesion to collagen via the α2β1 integrin and suggests that this regulation occurs by controlling the affinity state of the integrin.

The use of simulations and docking experiments revealed that Lys23 is a critical residue for controlling the affinity of ADP for ANT1, with the acetylated system having a much lower binding affinity for ADP.

We also show that the MCAK C terminus controls the affinity of full-length MCAK for microtubules and reduces its association with the lattice to ensure maximal recruitment to microtubule ends, where MCAK can act as a depolymerase.

Based on the CT domain controlling the affinity of MCAK for microtubules redundantly with the C-terminal tail of tubulin, we hypothesized that this electrostatically charged CT region may play also a role in MCAK diffusion on the lattice and targeting to microtubule ends.

In other words, Atg1 activation in yeast is apparently not exclusively controlled by regulated Atg13 binding, but rather involves additional levels of control, e.g., the affinity of the Atg1-Atg13 interaconformationalalterationseratiors, orecruitmentnt of additional factors regulated by the Atg13 phospho-status.

Disordered regions allow a thermodynamical control of the affinity and specificity of protein interactions.