| Range |
~100 sec^-1
|
| Organism |
Unspecified |
| Reference |
Laughlin SB, de Ruyter van Steveninck RR, Anderson JC. The metabolic cost of neural information. Nat Neurosci. 1998 May1(1):36-41 p.39 right column top paragraphPubMed ID10195106
|
| Primary Source |
Hua W, Young EC, Fleming ML, Gelles J. Coupling of kinesin steps to ATP hydrolysis. Nature. 1997 Jul 24 388(6640):390-3. AND Schnitzer, M.J. & Block, S.M. Kinesin hydrolyses one ATP per 8-nm step. Nature. 1997 Jul 24 388(6640):386-90.PubMed ID9237758, 9237757
|
| Method |
(2nd primary source:) Beads carrying single molecules of kinesin moving on microtubules were tracked with high spatial and temporal resolution by interferometry. Statistical analysis of the intervals between steps at limiting ATP, and studies of fluctuations in motor speed as a function of ATP concentration, allow the coupling ratio to be determined. |
| Comments |
"The motor protein kinesin cycles conformation approximately
100 times per second, hydrolyzing 1 ATP per cycle (primary sources)
and does considerable mechanical work." |
| Entered by |
Uri M |
| ID |
103551 |