User:Andy Maloney/Notebook/Lab Notebook of Andy Maloney/2009/09/02/Kinesin walking
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Today Larry and I discussed some of our thoughts on kinesin and how it walks along a microtubule. We discussed the paper I reviewed on Tuesday and revisited some of our initial questions. Those questions are:
- Is there a difference in the crystal structure of a kinesin foot when it has ATP or ADP bound?
- How do microtubule residues interact with kinesin's feet?
- How ATP and the "power stroke" are related.
- Does ATP interact with the residues on microtubules? If so, how.
- Is strain real? I.e. the strain felt in kinesin's legs.
- What is the persistence length for the legs of kinesin?
We talked about kinesin's neck linker and if it is shorter than the persistence length for the amino acid chains. We found several papers
that discuss this. It turns out that the length of the amino acid chains is longer than the persistence length of the chain and thus it is floppy.
