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The DNA-protein binding complexes were then analyzed on 5% polyacrylamide gel.
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RNA DNA hybrid-binding protein complexes were then eluted using RNA DNA hybrid oligonucleotides, with DNA DNA oligonucleotides as a control.
The predicted complexes were then subjected to cluster analysis under a pairwise binding site root mean squared deviation criterion.
Complexes were then subjected to SDS PAGE.
BAK complexes were then analyzed by SDS-PAGE.
The presence of cytokine/antibody complexes is then determined through binding to an immobilised capture antibody present on the array and subsequent streptavidin horseradish peroxidase and chemiluminescent detection.
These complexes are then loaded into nanocarriers.
The binding energy of the resulting complex is then estimated, considering the interactions between ligand and binding site.
The binding free energy for the complex is then evaluated.
The high-oligomer complex is then ready for Crm1 binding and nuclear export.
The mature complex is then established by the binding of a co-chaperone that bears a TPR (tetratricopeptide) repeat domain which interacts with Hsp90.
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