2000
DOI: 10.1038/35036345
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Force production by single kinesin motors

Abstract: Motor proteins such as kinesin, myosin and polymerase convert chemical energy into work through a cycle that involves nucleotide hydrolysis. Kinetic rates in the cycle that depend upon load identify transitions at which structural changes, such as power strokes or diffusive motions, are likely to occur. Here we show, by modelling data obtained with a molecular force clamp, that kinesin mechanochemistry can be characterized by a mechanism in which a load-dependent isomerization follows ATP binding. This model q… Show more

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Cited by 540 publications
(668 citation statements)
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“…The fore-dependence of the unbinding rate is described by an exponential increase with the absolute value of the force F, as suggested by experiments with kinesin-1 56 and by theory, 4 see Fig. 7c.…”
Section: Appendix A: Theoretical Description Of Single Motorsmentioning
confidence: 99%
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“…The fore-dependence of the unbinding rate is described by an exponential increase with the absolute value of the force F, as suggested by experiments with kinesin-1 56 and by theory, 4 see Fig. 7c.…”
Section: Appendix A: Theoretical Description Of Single Motorsmentioning
confidence: 99%
“…This feature has some interesting consequences for coupled motors that have been addressed experimentally in a recent study for two kinesins coupled via an antibody. 63 We note however that the run length becomes dependent on the ATP concentration if the ATP concentration is sufficiently low; 56 here, what concentration is sufficiently low depends on the concentration of inorganic phosphate in the buffer. 46 To discuss this issue within our theoretical framework, we consider a second mode of varying the single motor velocity.…”
Section: Control Of Travel Distance Through the Velocitymentioning
confidence: 99%
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“…The kinetic constants for fast axonal transport are expected to be at the high end of this range. Indeed, the average detachment rate from MTs for kinesin-1 is estimated to be 1 s −1 (Schnitzer et al [26], Vale et al [19]) while the average attachment rate for cytoplasmic dynein is estimated to be 1.5 s −1 (Carter and Cross [18], Vale et al [19]). However, the transition rate is expected to be smaller than these estimates because the transition involves detachment from MTs with plus-end-out orientation, switching of kinesin to dynein molecular motors, and then attachment to MTs with minus-end-out orientation.…”
Section: Resultsmentioning
confidence: 99%
“…The corresponding network of motor cycles provides a unified description for all motor properties that have been determined by single molecule experiments. For kinesin, the experimentally observed properties include motor velocity [9,16,17], bound state diffusion coefficient (or randomness parameter) [16], ratio of forward to backward steps [9], dwell time distributions [9], and run length [18] as functions of ATP concentration and load force as well as motor velocity as a function of P and ADP concentration [19].…”
Section: Introductionmentioning
confidence: 99%