Kinesin-1 and Eg5 are molecular motors that are essential for eukaryotic cell growth and development. Kinesin-1 motors transport intracellular cargo along the microtubule cytoskeleton through and against the dense viscoelastic cytoplasm. Eg5 motors mediate proper mitotic, microtubule spindle assembly during cell division, and stabilize these spindle structures with plus-end forces balancing opposing minus-end directed forces along the filaments. Therefore, it is important to understand how multiple kinesin-1 and Eg5 motors withstand competing forces, their structural rigidity under such loads, and how quickly they are able to rebind if loosed from their microtubule tracks. We get exact motor binding stoichiometry previously inaccessible by using a unique type of analysis for our optical trapping experiments. With this information, we characterize both motors and compare them to one another. We find the release forces for both types of motors add linearly with the number of motors bound and that Eg5 has a weaker binding than that of kinesin-1. The stiffness for the motor domains is comparable, yet we find that the average time to rebind for Eg5 decreases at higher concentrations while it does not for kinesin-1. This may indicate that there exists some weak interaction between kinesin-1 and microtubules keeping them close while unbound.