| Range |
>7 pN
|
| Organism |
Eukaryotes |
| Reference |
Gennerich A, Vale RD. Walking the walk: how kinesin and dynein coordinate their steps. Curr Opin Cell Biol. 2009 Feb21(1):59-67. doi: 10.1016/j.ceb.2008.12.002. p.59 right column 2nd paragraphPubMed ID19179063
|
| Primary Source |
Yildiz A, Tomishige M, Gennerich A, Vale RD. Intramolecular strain coordinates kinesin stepping behavior along microtubules. Cell. 2008 134: 1030–1041. doi: 10.1016/j.cell.2008.07.018. & Carter NJ, Cross RA. Mechanics of the kinesin step. Nature. 2005 435: 308–312.PubMed ID18805095, 15902249
|
| Comments |
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]." |
| Entered by |
Uri M |
| ID |
112202 |