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KINESIN. Microtubules. Questions. How much ATP is hydrolysed per step? How many rate-limiting steps are there? What is the mechanism of movement? Analyse movement Simulation of randomness. Michaelis-Menten kinetics. v = k cat [ATP]/(Km + [ATP])
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Questions • How much ATP is hydrolysed per step? • How many rate-limiting steps are there? • What is the mechanism of movement? Analyse movement Simulation of randomness
Michaelis-Menten kinetics v = kcat [ATP]/(Km + [ATP]) When [ATP] is limmiting: v = [ATP] kcat/Km – linear function Km: Michaelis constant: concentration of ATP at ½vmax kcat: Velocity at saturatet [ATP] Kinesin: Km = 62 +/- 8 µM kcat = 680 +/- 31 nm/s At limiting [ATP]: kcat/Km = 11 +/- 1 nm s-1 µM-1
Randomness parameter d = step distance x(t) = position r = 0: Clock-like r = 1: 1 rate-limiting step 0 < r < 1: more ratelimiting steps r > 1: increasing variance (backwards steps, double steps, biochemically inactivatet states)