Abstract
The 19F NMR spectra of the 5F-Trp labeled glutathione-S-transferase fusion protein with residues 282–595 of the human estrogen receptor show that there is a distinct conformational change in the protein when estradiol is added to the unliganded protein. Our studies show the empty receptor to have more conformational flexibility than the liganded form. This study shows the applicability of 19F NMR to study conformational change in large protein systems.
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