External mechanical force as an inhibition process in kinesin's motion.
We analysed published force-velocity data for kinesin using classical Michaelis-Menten kinetic theory and found that the effect of force on the stepping rate of kinesin is analogous to the effect of a mixed inhibitor in classical inhibition theory. We derived an analytical expression for the velocity of kinesin (the stepping rate, equal to the ATP turnover rate) as a function of ATP concentration and force, and showed that it accurately predicts the observed single molecule stepping rate of kinesin under a variety of conditions.
Ciudad
Aleix
A
Departament d'Estructura i Constituents de la Matèria, Facultat de Física, Universitat de Barcelona, Diagonal 647, 08028, Barcelona, Spain.
Sancho
José María
JM
D000255:Adenosine Triphosphate / Q000737:chemistry*; D001696:Biomechanical Phenomena; D016547:Kinesins / Q000737:chemistry*; D007700:Kinetics; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000737:chemistry; D011312:Pressure
D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D016547:Kinesins