The translocation of nucleic acid motor proteins along DNA or RNA can be studied in ensemble experiments by monitoring either the kinetics of the arrival of the protein at a specific site on the nucleic acid filament (generally one end of the filament) or the kinetics of ATP hydrolysis by the motor protein during translocation. The pre-steady state kinetic data collected in ensemble experiments can be analyzed by simultaneous global non-linear least squares (NLLS) analysis using a simple sequential "n-step" mechanism to obtain estimates of the rate-limiting step(s) in the translocation cycle, the average "kinetic step-size," and the efficiency of coupling ATP binding and hydrolysis to translocation. © 2009 Humana Press, a part of Springer Science+Business Media, LLC.
CITATION STYLE
Fischer, C. J., Wooten, L., Tomko, E. J., & Lohman, T. M. (2010). Kinetics of motor protein translocation on single-Stranded DNA. Methods in Molecular Biology, 587, 45–56. https://doi.org/10.1007/978-1-60327-355-8_4
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