Efficiency of kinesin under typical physiological conditions

Range 40-60 %
Organism Unspecified
Reference Lau AW, Lacoste D, Mallick K. Nonequilibrium fluctuations and mechanochemical couplings of a molecular motor. Phys Rev Lett. 2007 Oct 12 99(15):158102. p.158102-4 right column top paragraphPubMed ID17995215
Method "In a nutshell, FT [Fluctuation Theorem] states that the probability distribution for the entropy production rate obeys a symmetry relation, and it has been verified in a number of beautiful experiments on biopolymers and colloidal systems [ref 14]. In this Letter, [investigators] demonstrate that FT provides a natural framework in which thermodynamic constraints can be imposed on the operation of nanomachines far from equilibrium."
Comments "In particular, [investigators] find that T11 ~ 10T, the maximum value of ?? ~45 pN^-1s^-1, and ?? [the difference of the mechanochemical coupling coefficient] ~ -10 pN^-1s^-1 at large ?µ. Under typical physiological conditions (?? ~10–25kBT)[the chemical potential difference], kinesin operates at an efficiency in the range of 40 – 60%, also in agreement with experiments [J. Howard, Mechanics of Motor Proteins and the Cytoskeleton (Sinauer Associates, Sunderland, MA, 2001).]. Lastly, [investigators] point out a remarkable feature: the absolute maximum of ?m occurs approximately at a ?µ at which ?? is also a maximum, corresponding to an energy scale of 15–20kBT (see Fig.3). It is interesting to note that kinesins operate most efficiently in an energy scale corresponding to the energy available from ATP hydrolysis." Typical physiological conditions: ?µ~10–25kBT(Boltzman constant×Temperature (degree Kelvin))
Entered by Uri M
ID 103008