13_-_Motors_and_muscles

13_-_Motors_and_muscles - BMEN E4001x: Quantitative...

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BMEN E4001x: Quantitative Physiology I / Molecular and Cellular Systems Notes 13 – Motors and muscles Sources for this section: Nelson: Section 10.4 Tubulin - kinesin: (We’ll focus on kinesin, as it is better understood) With ATP, kinesin moves one step along microtubule (~8nm), even with large loads. Suggests tight coupling between motor protein and microtubule. As a chemical reaction, can expressed as movement ADP K M ATP K M + + + + + and in this respect, is an enzymatic reaction. Let’s look a bit closer, first by rewriting as: movement ADP K M ATP K M ATP K M 2 1 1 k k k + + →   → + - ATP binding is purely chemical, but there is a power stroke that accompanies hydrolysis. This would suggest a MM-type response with respect to ATP, and indeed, it is superficially seen to be true.
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The different lines indicate different loads. Each load exhibits MM-type behavior, as seen from both types of plots. (slope=K M /vmax). Something is wrong here when we look at the inclusion of motion, however. Let’s start with some actual values:
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13_-_Motors_and_muscles - BMEN E4001x: Quantitative...

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