Final answer:
Kinesin 1 and myosin II share several features, but only myosin II can form bipolar filaments, which are crucial for muscle contraction; kinesin 1 does not have this capability.
Step-by-step explanation:
The feature that kinesin 1 and myosin II do not share is the formation of bipolar filaments. While kinesin 1 and myosin II share traits like plus-end directed motor activity, two heads, dimer formation by heavy chain tails, and ATPase activity, only myosin II is capable of forming bipolar filaments.
Myosin II forms part of the thick filament in muscle cells, and it's structured in such a way that it can form bipolar filaments, which are essential for contraction in muscle cells. Kinesin 1, on the other hand, moves along microtubules and does not form bipolar filaments. This fact underscores the unique roles these motor proteins play in cell motility and transport.
Both myosin II and kinesin 1 use ATP hydrolysis to power movement, with myosin II moving along actin filaments, and kinesin 1 moving along microtubules. Myosin II forms a part of the mechanism of muscle contraction, while kinesin 1 is primarily involved in the transport of vesicles and organelles within the cell.
Kinesin 1 and myosin II share several features, such as plus end directed motor activity, formation of bipolar filaments, and ATPase activity. However, they differ in terms of their structure. While myosin II forms dimers with heavy chain tails coiled around each other, kinesin 1 does not have this specific structural feature. Therefore, dimers formed by heavy chain tails coiled around each other.