Abstract
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.