Estrogen functions by binding to receptors that control gene transcription, leading to the creation of proteins that regulate several functions within an organism. The hormone/receptor binding event can be blocked by the binding of molecules that are structurally similar to estrogen, causing various developmental issues, specifically causing damage to the ovarian follicles. There is a gap current literature that would offer a solution as to how conformational changes in proteins can be caused by the binding of incorrect ligands, triggering the proteins to function differently. Glycitein, a phytoestrogen found in soy, is used to characterize the effects of phytoestrogens on cell signaling with estrogen receptor beta (ER�), using rats as a model system. The ligand binding domain (LBD) of rat ER� was subcloned using PCR. Escherichia coli is ideal for bacterially expressing rER� LBD. Isothermal calorimtry can be used to determine the binding affinity for estrogen and glycitein.

Determination of the binding constant when glycitein is complexed with rat estrogen receptor beta

245th National Meeting (2013)

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