Abstract
Several biological molecular motors, for instance kinesin and non-claret disjunctional (ncd), belonging to the same superfamily of motor proteins move towards opposite ends of microtubules. It is clear that motor protein motion is powered through ATP hydrolysis, but neither the specifics of the chemical to mechanical energy transduction nor the molecular basis for motion directionality are precisely known. While the protein catalytic domain seems to be responsible for the processibility of the motor on the microtubule, the "neck" region adjacent to the motor heads was found recently to control the directionality of movement. We show here that a simple Newtonian model of two motor head particles connected through a neck coiled-coil spring whose rest length changes with each ATP hydrolysis event captures the essential motor dynamics features. In particular, the observed directionality reversal in chimaeras with different coiled-coil regions results in the model from a change in the stiffness of the spring coefficient. We find that motor speed is determined by the average ATP absorption rate while the effect of ambient temperature is relatively small, leading to essentially non-Brownian, deterministic motor motion.
| Original language | English |
|---|---|
| Pages (from-to) | 151-156 |
| Number of pages | 6 |
| Journal | Physics Letters, Section A: General, Atomic and Solid State Physics |
| Volume | 252 |
| Issue number | 3-4 |
| Publication status | Published - Feb 22 1999 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Physics and Astronomy(all)
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Directional Newtonian motion and reversals of molecular motors. / Stratopoulos, G. N.; Dialynas, T. E.; Tsironis, G. P.
In: Physics Letters, Section A: General, Atomic and Solid State Physics, Vol. 252, No. 3-4, 22.02.1999, p. 151-156.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Directional Newtonian motion and reversals of molecular motors
AU - Stratopoulos, G. N.
AU - Dialynas, T. E.
AU - Tsironis, G. P.
PY - 1999/2/22
Y1 - 1999/2/22
N2 - Several biological molecular motors, for instance kinesin and non-claret disjunctional (ncd), belonging to the same superfamily of motor proteins move towards opposite ends of microtubules. It is clear that motor protein motion is powered through ATP hydrolysis, but neither the specifics of the chemical to mechanical energy transduction nor the molecular basis for motion directionality are precisely known. While the protein catalytic domain seems to be responsible for the processibility of the motor on the microtubule, the "neck" region adjacent to the motor heads was found recently to control the directionality of movement. We show here that a simple Newtonian model of two motor head particles connected through a neck coiled-coil spring whose rest length changes with each ATP hydrolysis event captures the essential motor dynamics features. In particular, the observed directionality reversal in chimaeras with different coiled-coil regions results in the model from a change in the stiffness of the spring coefficient. We find that motor speed is determined by the average ATP absorption rate while the effect of ambient temperature is relatively small, leading to essentially non-Brownian, deterministic motor motion.
AB - Several biological molecular motors, for instance kinesin and non-claret disjunctional (ncd), belonging to the same superfamily of motor proteins move towards opposite ends of microtubules. It is clear that motor protein motion is powered through ATP hydrolysis, but neither the specifics of the chemical to mechanical energy transduction nor the molecular basis for motion directionality are precisely known. While the protein catalytic domain seems to be responsible for the processibility of the motor on the microtubule, the "neck" region adjacent to the motor heads was found recently to control the directionality of movement. We show here that a simple Newtonian model of two motor head particles connected through a neck coiled-coil spring whose rest length changes with each ATP hydrolysis event captures the essential motor dynamics features. In particular, the observed directionality reversal in chimaeras with different coiled-coil regions results in the model from a change in the stiffness of the spring coefficient. We find that motor speed is determined by the average ATP absorption rate while the effect of ambient temperature is relatively small, leading to essentially non-Brownian, deterministic motor motion.
UR - http://www.scopus.com/inward/record.url?scp=0041708489&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0041708489&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0041708489
VL - 252
SP - 151
EP - 156
JO - Physics Letters, Section A: General, Atomic and Solid State Physics
JF - Physics Letters, Section A: General, Atomic and Solid State Physics
SN - 0375-9601
IS - 3-4
ER -