GAK protein was immobilized on a capillary HPLC column, and compound binding was characterized by frontal affinity chromatography.
This binding mechanism is characterized by multiple weak binding sites that have fast off rates, such that when the number of binding moieties increases, the apparent binding affinity may also increase.
The ligand binding site is characterized by a constrained size of the cavity and the requirement for both an acidic group and a hydrophobic group in the ligand (Fig. 3C).
The EB binding region is characterized by enhanced lateral interprotofilament contacts that protect the microtubule from depolymerization.
The AR-like binding site is characterized by the highest affinity for T (IC50, 849 nM), followed by displacement effects about one order of magnitude lower for the androgen MT as well as for E2.
The STAT-3 binding site is characterized by a position weight matrix of 21 base pair length in the TRANSFAC database (Accession number M00225), with a position weight matrix similarity threshold of 0.934 for minimizing false positives in finding the binding site on genomic sequences.
Moreover, calorimetric titrations revealed UP1 binds SL3ESS3 as a high-affinity (Kd = 37.8 ± 1.1 nM) 1 1 complex, where the binding profile is characterized by a large favorable change in enthalpy (Δ H° = −38.8 ± 2.1 kcal/mol) and opposed by an unfavorable change in entropy (− TΔ S° = 28.7 ± 2.1 kcal/mol).
This Hfq binding motif is characterized by U-rich regions, specifically a poly-U tail at the 3' end of the sRNA (downstream of the Rho independent terminator), and the U-rich or the AU-rich region upstream of the rho-independent terminator or other secondary hairpin structure; the 5' region of the sRNA is involved in (non-perfect) base-pairing with the target mRNA [ 52, 53, 55].
This family of DNA-binding proteins is characterized by the presence of one or two (Cys)4 metal binding sites which recognize the protein's eponymous binding site, GATA.
