# User:TheLarry/Notebook/Larrys Notebook/2010/08/23

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## Rate Constants

Yesterday i reported that my model was not following the proper michaelis menten kinetics. at low atp the velocity stayed high. So it was unbinding quickly but taking a step or so keeping the velocity high. it is possible that the kinesin needs to waste more time before disassociating, but i am not sure. today i am gonna go over rate constants that are not in my pdf file that josey helped me compile

### Monomer

• Interacting Head Mechanism of Microtubule-Kinesin ATPase, Ma and Taylor
• ADP binding: 1.5 $\displaystyle{ \mu M^{-1}s^{-1} }$
• ADP dissociation: $\displaystyle{ 110 s^{-1} }$

• $\displaystyle{ .25 \mu M^{-1} s^{-1} }$