Renewal processes and fluctuation analysis of molecular motor stepping.
We present a systematic method of analysis of experiments performed with single motor proteins. The use of such a method should allow a more detailed description of the motor's chemical cycle through the precise fitting of the experimental data. We model the dynamics of a processive or rotary molecular motor using a renewal process, in line with the work initiated by Svoboda, Mitra and Block. We apply a functional technique to compute different types of multiple-time correlation function of the renewal process, which have applications to bead-assay experiments performed both with processive molecular motors, such as myosin V and kinesin, and rotary motors, such as F1-ATPase.
Santos
Jaime E
JE
Hahn-Meitner Institut, Abteilung Theorie, Glienicker Str. 100, D-14109 Berlin, Germany.
Franosch
Thomas
T
Parmeggiani
Andrea
A
Frey
Erwin
E
D016547:Kinesins / Q000737:chemistry; D008956:Models, Chemical; D020409:Molecular Motor Proteins; D024701:Myosin Type V / Q000737:chemistry; D006180:Proton-Translocating ATPases / Q000737:chemistry
D020409:Molecular Motor Proteins; D024701:Myosin Type V; D006180:Proton-Translocating ATPases; D016547:Kinesins