Two-thirds of disease-associated mutations disrupt protein complexes, yet thereislittlequantitative informationabout the equilibrium thermodynamics of complex formation in cells. We arequantifying the dissociation constant of a protein-protein interaction in Escherichiacolicellsusingafluorine-labeled variantoftheB1 domainofproteinGthat formsadomain-swappedhomodimer. We are using 19F NMR to quantify the amounts of monomer and dimer, Tuner(DE3)tm cells to modulate GB1 concentration, and a combination of LC-MS and flow cytometry to measure the GB1 concentration in cells.

Quantifying a protein-protein interaction in living cells

2019 Fall National Meeting

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