Print Email Facebook Twitter Kinetic analysis methods applied to single motor protein trajectories Title Kinetic analysis methods applied to single motor protein trajectories Author Nord, A. L. (Université de Montpellier) Pols, AAJ (Student TU Delft; Kavli institute of nanoscience Delft) Depken, S.M. (TU Delft BN/Martin Depken Lab; Kavli institute of nanoscience Delft) Pedaci, F. (Université de Montpellier) Date 2018 Abstract Molecular motors convert chemical or electrical energy into mechanical displacement, either linear or rotary. Under ideal circumstances, single-molecule measurements can spatially and temporally resolve individual steps of the motor, revealing important properties of the underlying mechanochemical process. Unfortunately, steps are often hard to resolve, as they are masked by thermal noise. In such cases, details of the mechanochemistry can nonetheless be recovered by analyzing the fluctuations in the recorded traces. Here, we expand upon existing statistical analysis methods, providing two new avenues to extract the motor step size, the effective number of rate-limiting chemical states per translocation step, and the compliance of the link between the motor and the probe particle. We first demonstrate the power and limitations of these methods using simulated molecular motor trajectories, and we then apply these methods to experimental data of kinesin, the bacterial flagellar motor, and F1-ATPase. To reference this document use: http://resolver.tudelft.nl/uuid:eac7a793-4119-41d8-ae22-6db4913cd328 DOI https://doi.org/10.1039/c8cp03056a ISSN 1463-9076 Source Physical chemistry chemical physics (PCCP), 20 (27), 18775-18781 Part of collection Institutional Repository Document type journal article Rights © 2018 A. L. Nord, AAJ Pols, S.M. Depken, F. Pedaci Files PDF c8cp03056a.pdf 2.11 MB Close viewer /islandora/object/uuid:eac7a793-4119-41d8-ae22-6db4913cd328/datastream/OBJ/view