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||P.2 2nd paragraph:"Kinesin is composed of two identical heavy chains (HCs) and two associated light chains (Figure 1a) [ref 1]. Each HC includes an N-terminal motor domain that houses catalytic activity followed by a coiled-coil stalk that facilitates dimerization. While stepping, ATP hydrolysis is coupled to an 8 nm center-of-mass displacement (Figure 2a) [BNID 112201], the distance between adjacent tubulin heterodimers. While kinesin predominantly takes forward steps along a single MT protofilament [refs 16,17,18••], an opposing force increases the probability of rearward stepping, and kinesin can walk backward at loads exceeding 7 pN [primary sources]."