User:Andy Maloney/Osmotic stress effects on kinesin and microtubules

Motivation
The molecular motor kinesin-1, an ATPase, and the substrate it walks along, microtubules, are vital components of eukaryotic cells. Kinesin converts chemical energy to linear motion as its two motor domains step along microtubules in a process similar to how we walk. Cells create systems of microtubules that direct the motion of kinesin. This directed motion allows kinesin to transport various cargoes inside cells.

During the stepping process, the kinesin motor domains bind and unbind from their binding sites on microtubules. Binding and unbinding rates of biomolecules are highly dependent on hydration and exclusion of water from the binding interface. Osmotic stress will likely strongly affect the binding and unbinding rates for kinesin and thus offers a tool to specifically probe those steps. This research is designed to investigate how different osmotic stressing agents affect how kinesin's motor domains bind and unbind from their binding sites on microtubules.

Notebook
Below you will find a list of my notebook entries related to investigating kinesin and microtubules under osmotic stress.