| 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)) |