Even though we neglect information on binding events caused by OCT4-DNA interactions mediated by unknown cofactors and heterodimer complexes, our results reflect confirmed functional circuitries dependent on direct OCT4 and SOX-OCT binding.
The altered conformational flexibility, the degree of correlated motion between residues in the Fas DD, hydrogen bond formation within the CaM binding region, the contact number of each residue, and the electrostatic potential for the CaM binding region caused by the Fas DD V254N mutation could influence the van der Waals interactions and electrostatic interactions between CaM and the Fas DD.
As suggested from the dimeric nature of the ligands, binding to immobilized receptors shows avidity due to cooperative binding caused by bivalent ligand-receptor interactions.
We used the drkEOA mutant, which loses binding to EGFR caused by mutation in the SH2 domain [39], for a genetic interaction assay.
Unlike the SPR signal, the impedance response is not scaled with the mass of analyte molecule and is insensitive to nonspecific bindings caused by electrostatic interactions.
The reduction in the binding rate under strong nonnative hydrophobic interactions was caused by non-specific kinetic traps along the binding trajectory.
The substrate-binding amino acids are located in loops extending from the 8 barrel fold, and in some chitinases, additional interactions are caused by an extra domain existing as a barrel insertion (Lienemann et al. 2009).
In many cases, the interactions are caused by caffeine.
A direct interaction is usually caused by protein-ligand binding, whereas an indirect interaction can be induced by the changed expression level of a protein or active metabolites produced by a drug.
However, the SO interaction causes the binding energy of ununtrium monohydride to be reduced by about 1 eV and the ununtrium hydrogen bond length to decrease as the bonding 7p1/2 orbital is relativistically contracted.
