| Thermodynamic and kinetic parameters for substrate binding to the Tetrahymena ribozyme are studied with pyrene labeled substrates and rapid mixing fluorescence-detected stopped-flow.;The rates of docking and undocking of substrate, pyrCUCU, to the catalytic core of the Tetrahymena ribozyme as a function of temperature are reported. The results indicate docking is associated with a large activation energy. The activation enthalpy, ;The rate constants of association and dissociation of pyrCUCUA are reported at 10 mM Mg;The effects of Mg;Comparisons of results with prG and pdG indicate the 2... |
