Abstract
AbstractSynthetic, structural, and computational approaches were used to solve the puzzle as to how a phenolic nonsteroidal estrogen 1 with only a single H‐bond to its receptor was more potent than an isomer 2 which formed an intricate network of H‐bonds. Synthesis of a series of substituted phenols revealed that pKa was not a determinant of estrogenic activity. First‐principles calculation also failed to explain the difference in activity of 1 and 2. Molecular dynamics revealed that 1 formed a more stable receptor complex compared to 2, which may explain its increased activity despite forming fewer apparent H‐bonds with the protein.
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