Kinetics of motor protein translocation on single-Stranded DNA

Christopher J. Fischer, Lake Wooten, Eric J. Tomko, Timothy M. Lohman

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

14 Scopus citations


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.

Original languageEnglish
Title of host publicationHelicases
Subtitle of host publicationMethods and Protocols
Number of pages12
StatePublished - 2010

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • ATPase
  • Translocase
  • helicase
  • kinetics
  • motor protein


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