The stalk of the ATPase structure is similar to the twisted pair of protein stra
ID: 1778968 • Letter: T
Question
The stalk of the ATPase structure is similar to the twisted pair of protein strands that make up the motor feet of the kinesin. The twisted proteins act like a spring system, storing elastic potential energy as it twists or untwists from its equilibrium state. The energy function for this system is shown in the figure below right where the energy is given in multiples of T. If the mechanical energy of the kinesin stalk is 150 k.T, to what angular range is the stalk 4. confined? Energy, E. (#4T) os Angular Twist, A0, (rad) s. The rotor portion of the cytosolic complex can be modeled as .aT Tited top view ring thick-walled ring, 13.0 nm across and having a central hole which is 4.0 nm across.4 The mass of the ring complex is 2.355x102 kg. What is the approximate moment of inertia of the ring? Side view Side view- slab o Xulish, AD. Wright, &E.M.Terentjev.; Fi rotary motor of ATP synthase is driven by the torsionally-asymmetric drive shaft. NatureExplanation / Answer
router = outer radius = 13 /2 = 6.5 nm = 6.5 x 10-9 m
rinner = inner radius = 4 /2 = 2 nm = 2 x 10-9 m
m = mass of ring = 2.355 x 10-22 kg
moment of inertia is given as
I = (0.5) m (router2 + rinner2)
I = (0.5) (2.355 x 10-22) ((6.5 x 10-9)2 + (2 x 10-9)2)
I = 5.45 x 10-39
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