Kinetics of the E. coli replication factor DnaC protein-nucleotide interactions. II. Fluorescence anisotropy and transient, dynamic quenching stopped-flow studies of the reaction intermediates.

@article{Galletto2002KineticsOT,
  title={Kinetics of the E. coli replication factor DnaC protein-nucleotide interactions. II. Fluorescence anisotropy and transient, dynamic quenching stopped-flow studies of the reaction intermediates.},
  author={Roberto Galletto and Wlodzimierz Bujalowski},
  journal={Biochemistry},
  year={2002},
  volume={41 28},
  pages={8921-34}
}
The nature of the intermediates in the binding of MANT-ATP and MANT-ADP to the E. coli replicative factor DnaC protein (accompanying paper) has been examined using the fluorescence intensity, anisotropy, and transient dynamic quenching stopped-flow techniques. Using molar fluorescence intensities of individual intermediates of the reaction, we derived the Stern-Volmer equation that provides a direct method to quantitatively address the quenching of the fluorescence of a transient intermediate… CONTINUE READING