This thesis reports on the analysis of proteins with electrically switchable DNA layers. The
switchSENSE platform provides a simultaneous quantification of binding kinetics, protein size and protein charge. The switching velocity of protein-DNA complexes under applied
AC potentials is measured to monitor protein binding and to quantify binding parameters (
kon,
koff, and
KD). A comparison of the time resolved DNA switching dynamics with simulations yields the hydrodynamic radius of the bound protein. The protein charge and isoelectric point are inferred from pH dependent measurements of the DNA conformation as a function of applied potential. Moreover, the interaction of transcription factors with recognition sequences along DNA templates is characterized. The merits of voltage-mediated DNA conformation control for the detection of protein induced DNA bending are described.
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This thesis reports on the analysis of proteins with electrically switchable DNA layers. The
switchSENSE platform provides a simultaneous quantification of binding kinetics, protein size and protein charge. The switching velocity of protein-DNA complexes under applied
AC potentials is measured to monitor protein binding and to quantify binding parameters (
kon,
koff, and
KD). A comparison of the time resolved DNA switching dynamics with simulations yields the hydrodynamic radius of the bound prot...
»