A unified phenomenological analysis of the experimental velocity curves in molecular motors.
We present a unified phenomenological kinetic framework to analyze the experimental data of several motor proteins (either linear or rotatory). This formalism allows us to discriminate the characteristic times of most relevant subprocesses. Explicitly, internal mechanical as well as chemical times are taken into account and joined together in a full-cycle time where effusion, diffusion and chemical rates, viscoelastic friction, and overdamped motion are considered. This approach clarifies the most relevant mechanisms in a particular motor by using the available experimental data of velocity versus external load and substrate concentration. We apply our analysis to three real molecular motors for which enough experimental data are available: the bacterial flagellar motor [Yoshiyuki et al., J. Mol. Biol. 377, 1043 (2003)], conventional kinesin (kinesin-1) [Block et al., Proc. Natl. Acad. Sci. U.S.A. 100, 2351 (2003)], and a RAN polymerase [Abbondanzieril, Nature (London) 438, 460 (2003)]. Moreover, the mechanism of stalling a motor is revised and split into two different concepts (mechanical and chemical stalling) that shed light to the understanding of backstepping in kinesin-1.
Ciudad
Aleix
A
Department d'Estructura i Constituents de la Matèria, Facultat de Física, Universitat de Barcelona, Diagonal 647, E-08028 Barcelona, Spain. aleixciudad@gmail.com
Sancho
J M
JM
D001426:Bacterial Proteins; D001696:Biomechanical Phenomena; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D016547:Kinesins / Q000378:metabolism; D007700:Kinetics; D020409:Molecular Motor Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D020409:Molecular Motor Proteins; D012321:DNA-Directed RNA Polymerases; D016547:Kinesins