The mechanism of rectified Brownian movement is used to analyze measured da
ta for kinesin motion along microtubules. A key component of the mechanism
is the diffusive movement of the microtubule binding heads of kinesin durin
g the adenosine triphosphate (ATP) cycle. The first-passage time distributi
on for this step is analyzed in detail and is shown to be responsible for o
bserved load-velocity profiles. The ATPase activity of the kinesin heads is
that of a nucleotide switch and not that of a direct chemomechanical energ
y converter. Experimental data acquisition, rate constants, and alternative
explanations are discussed. The mechanism described in this paper is funda
mental to the nanobiology of intracellular processes.