Research
Conformational dynamics and ensembles
How changes in structural motions (dynamics) connect ligand binding to shifting nuclear receptor conformational ensembles and changes in function.
Proteins populate multiple conformations. We investigate how ligands alter nuclear receptor conformational ensembles and how those changes influence interactions with coactivators and corepressors.
Studies of PPARγ connect transcriptional activation and repression with the behavior of its activation surface. NMR spectroscopy and structural approaches help reveal the molecular mechanisms behind graded agonism and inverse agonism.
