Abstract
The two-headed motor protein kinesin hydrolyzes ATP and moves on microtubule tracks towards the plus end. The motor develops speeds and forces of the order of hundreds of nanometers per second and piconewtons, respectively. Recently, the dependence of the velocity, the dissociation rate and the displacement variance on the load and the ATP concentration were measured in vitro for individual kinesin molecules (Coppin et al., 1997; Visscher et al., 1999) over a wide range of forces. The structural changes in the kinesin motor that drive motility were discovered by Rice et al. (1999). Here we present a phenomenological model for force generation in kinesin based on the bi-stable, nucleotide-dependent behavior of the neck linker. We demonstrate that the model explains the mechanical, kinetic and statistical (experimental) data of Coppin et al. (1997). We also discuss the relationship between the model results and experimental data of Visscher et al. (1999).
| Original language | English (US) |
|---|---|
| Pages (from-to) | 143-157 |
| Number of pages | 15 |
| Journal | Journal of Theoretical Biology |
| Volume | 211 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jul 21 2001 |
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ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
Cite this
Structural changes in the neck linker of kinesin explain the load dependence of the motor's mechanical cycle. / Mogilner, A.; Fisher, Andrew J; Baskin, R. J.
In: Journal of Theoretical Biology, Vol. 211, No. 2, 21.07.2001, p. 143-157.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structural changes in the neck linker of kinesin explain the load dependence of the motor's mechanical cycle
AU - Mogilner, A.
AU - Fisher, Andrew J
AU - Baskin, R. J.
PY - 2001/7/21
Y1 - 2001/7/21
N2 - The two-headed motor protein kinesin hydrolyzes ATP and moves on microtubule tracks towards the plus end. The motor develops speeds and forces of the order of hundreds of nanometers per second and piconewtons, respectively. Recently, the dependence of the velocity, the dissociation rate and the displacement variance on the load and the ATP concentration were measured in vitro for individual kinesin molecules (Coppin et al., 1997; Visscher et al., 1999) over a wide range of forces. The structural changes in the kinesin motor that drive motility were discovered by Rice et al. (1999). Here we present a phenomenological model for force generation in kinesin based on the bi-stable, nucleotide-dependent behavior of the neck linker. We demonstrate that the model explains the mechanical, kinetic and statistical (experimental) data of Coppin et al. (1997). We also discuss the relationship between the model results and experimental data of Visscher et al. (1999).
AB - The two-headed motor protein kinesin hydrolyzes ATP and moves on microtubule tracks towards the plus end. The motor develops speeds and forces of the order of hundreds of nanometers per second and piconewtons, respectively. Recently, the dependence of the velocity, the dissociation rate and the displacement variance on the load and the ATP concentration were measured in vitro for individual kinesin molecules (Coppin et al., 1997; Visscher et al., 1999) over a wide range of forces. The structural changes in the kinesin motor that drive motility were discovered by Rice et al. (1999). Here we present a phenomenological model for force generation in kinesin based on the bi-stable, nucleotide-dependent behavior of the neck linker. We demonstrate that the model explains the mechanical, kinetic and statistical (experimental) data of Coppin et al. (1997). We also discuss the relationship between the model results and experimental data of Visscher et al. (1999).
UR - http://www.scopus.com/inward/record.url?scp=0035928490&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035928490&partnerID=8YFLogxK
U2 - 10.1006/jtbi.2001.2336
DO - 10.1006/jtbi.2001.2336
M3 - Article
C2 - 11419956
AN - SCOPUS:0035928490
VL - 211
SP - 143
EP - 157
JO - Journal of Theoretical Biology
JF - Journal of Theoretical Biology
SN - 0022-5193
IS - 2
ER -