Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements.

The anisotropy decay curves displayed three important features: first, the φ 2 values were expectedly much longer than the ones obtained for the DDM micelles using the free TMR-M dye (φ 2 ~28 ns, Figure S5 ) since now the fluorophore is covalently linked to the protein; in addition, there was a clear trend for an increase of φ 2 with pH ( Table 1 ).

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