Abstract
The chapter analyzes the binding and dissociation of TATA human box-binding protein in solution to ERα-N immobilized on a surface plasmon resonance (SPR) biosensor surface, and the binding and dissociation of estradiol in solution to glutathione-S-transferase (GST)-thyroid hormone associated protein (TRAP) 220 and GST-transcriptional intermediary factor (TIF2) immobilized on an SPR biosensor surface. Binding and dissociation rate coefficients, and affinity values, as well as fractal dimension values, are obtained in the chapter. The chapter presents a fractal analysis for the binding of estrogen receptors in solution to different ligands immobilized on a SPR biosensor chip surface. The fractal analysis takes into account the effect of the surface heterogeneity on the diffusion-limited biomolecular interaction kinetics. Both single- and dual-fractal models are employed to model the binding and dissociation kinetics. It should be kept in mind that different laboratories use different technologies, slightly different technologies, or different experimental designs to analyze the affinity of ligands or cofactors to target proteins (or analytes) of interest.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
