Kinesins typically consist of two large globular heads that allow attachment to microtubules, a central coiled region, and a region termed light-chain, which connects the kinesin to the intracellular component to be moved.


A polystyrine bead / kinesin / ATP combination was used to evaluate the velocity of kinesin anterograde transport (8nm per step, 2 micrometers per second), and both glass fibre and optical techniques were used to evaluate the force associated with this (>8 pN forward), see references 1,2.

The movement described as walking involves one of the two globular heads moving forward, and making an attachment with a beta-tubulin molecule. As this bond is made, ATP is hydrolyzed, giving energy required to break the bond associated with the other globular head. In this way the molecule can process for distances as far as 1 micrometer.

The process of kinesin movement is ATP dependant, and is about 60-70% efficient.

Kinesin is in fact a family of proteins, including some which move towards the negative end of the MT. These different Kinesins act for different purposes, and have different structures, including mitosis and meiosis.

References

1.
Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2351-6. Epub 2003 Feb 18 : Probing the kinesin reaction cycle with a 2D optical force clamp : Block SM, Asbury CL, Shaevitz JW, Lang MJ.

2.
Biophys J. 1996 Dec;71(6):3467-76 : Kinesin force generation measured using a centrifuge microscope sperm-gliding motility assay : Hall K, Cole D, Yeh Y, Baskin RJ.

3.
Benjamin Cummings 2003 : The World of The Cell : Becker, Kleinsmith, Harding