RISC Kinetic and Thermodynamic Data
Published: 24 July 2019| Version 1 | DOI: 10.17632/fzh7pfpmmb.1
Contributor:
Winston BeckerDescription
We applied high-throughput methods to measure the association kinetics, equilibrium binding energies, and single- turnover cleavage rates of RISC. We find that RISC readily tolerates insertions of up to seven nucleotides in its target opposite the central region of the guide. Fit parameters for miR-21 and let-7a association, equilibrium binding, and cleavage are provided herein. These data were obtained from RNA-MaP and RISC Cleave-'n-Seq. Raw sequencing data is available on SRA.
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Biochemistry