Sharona E. Gordon

This paper introduces a method to adjust tmFRET distance sensitivity using different metal ions at a single bpyA-labeled protein site, enabling conformational change measurements.

This study uses fluorescent noncanonical amino acids to measure conformational changes in hHv1, showing Zn2+ induces reversible FRET changes.

This study uses tmFRET to analyze GTP-coupled conformational changes in Mfn1, revealing an unexpected conformational reversal and heterogeneous transition-state ensemble.

This study uses time-resolved tmFRET to analyze conformational changes and energetics in the CNBD of SthK, showing that transmembrane domains make the activating conformation more favorable.

This study uses time-resolved tmFRET to analyze conformational changes and energetics in the SthK C-terminal region upon cAMP and cGMP binding, revealing large structural changes with cAMP and partial agonism with cGMP.

This paper expands the working distance of tmFRET to 50 Å using new ligands, enabling precise measurement of conformational changes in maltose binding protein under physiological conditions.

This paper develops a fluorescence method to measure protein conformational dynamics and energetics using time-resolved tmFRET and validates it with EPR spectroscopy.

The paper uses optogenetic PI3K activation and genetic code expansion to study RTK signaling, showing PI3K alone can traffic TRPV1 and insulin receptors to the plasma membrane.