Triplet tumbling microscopy enables in situ quantification of protein complex assembly and dynamics

Triplet tumbling microscopy (TTM) enables real-time in-cell quantification of protein complex assembly and dynamics by reporting complex size from rotational diffusion.

• Why it matters: Measuring protein-protein interactions in cells has been constrained by limited scope and the need for prior knowledge of interacting partners.
• What they did: TTM uses infrared-triggerable triplet-state emission to infer protein complex size from tumbling via rotational diffusion, overcoming fluorescence anisotropy size limits.
• The result: In cells, TTM detects PPIs, quantifies bound fractions, and distinguishes complexes by size, including rapamycin-induced dimerization, p53 homo-oligomerization, and E6AP binding to human papilloma virus 16 E6.

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