William N. Zagotta

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.