Rate in which kinesin motor protein cycles conformation

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