Since BSA binds fatty acids [ 24], it was plausible that the binding of the BSA conjugates to the free trityl side product decreased the water solubility of the BSA.
These values are of similar magnitude to experimental ones but do not predict correctly that the binding of the c-Jun c-Jun homodimer is stronger.
This suggests that the binding of the glycoside-bearing HPMA copolymer DOX conjugates to the cells was mediated not only by galectin-3.
It was observed that the binding of the inhibitor 2-aminoperimidine established interactions different from those introduced by the binding of the native ligand.
The strong quenching of the fluorescence clearly indicated that the binding of the drug to HSA changed the microenvironment of tryptophan residue and the tertiary structure of HSA.
Results show that the binding of the GPI-anchored protein is specifically occurring through an interaction between the GPI-anchor and the albumin microparticle surface.
Additionally, we present the results of limited proteolysis studies that demonstrate that the binding of the novel acyl-adenylate analog protects luciferase from proteolysis.
It was found that the binding of the fluorescent beads saturated when a 10-fold or higher molar ratio of biotin to antibody was used.
Circular dichroism (CD) measurements indicate that the binding of the protein to CNT does not alter the excitonic interactions, i.e. there is no substantial change in the RC structure after the binding [24].
This phenomenon also clearly indicates that the binding of the CEM-aptamer complex to the aptamer is weaker than that of GO, thus allowing the aptamer to fall off the surface of GO.
Finally, our data also show that the binding of the nanobody does not alter the secondary structure content of the stRNA as well as its unfolding/refolding processes during heat treatment.
