dorsal/arxiv
View SchemaMechanism of unidirectional movement of kinesin motors
| Authors | Ping Xie, Shuo-Xing Dou, Peng-Ye Wang |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0312043 |
| URL | https://arxiv.org/abs/q-bio/0312043 |
| DOI | 10.1088/1009-1963/14/4/017 |
| Journal | Chinese Physics, Vol.14, No.4 (2005) 734-743 |
Abstract
Kinesin motors have been studied extensively both experimentally and theoretically. However, the microscopic mechanism of the processive movement of kinesin is still an open question. In this paper, we propose a hand-over-hand model for the processivity of kinesin, which is based on chemical, mechanical, and electrical couplings. In the model the processive movement does not need to rely on the two heads' coordination in their ATP hydrolysis and mechanical cycles. Rather, the ATP hydrolyses at the two heads are independent. The much higher ATPase rate at the trailing head than the leading head makes the motor walk processively in a natural way, with one ATP being hydrolyzed per step. The model is consistent with the structural study of kinesin and the measured pathway of the kinesin ATPase. Using the model the estimated driving force of ~ 5.8 pN is in agreements with the experimental results (5~7.5 pN). The prediction of the moving time in one step (~10 microseconds) is also consistent with the measured values of 0~50 microseconds. The previous observation of substeps within the 8-nm step is explained. The shapes of velocity-load (both positive and negative) curves show resemblance to previous experimental results.
{
"annotation_id": "9f4410d6-5447-45b0-8bb8-982bedbe510e",
"date_created": "2026-03-02T18:01:30.963000Z",
"date_modified": "2026-03-02T18:01:30.963000Z",
"file_hash": "18ea24b73df8c329e3e6e8d1ac2211eee4f110325b409b2dcaccb7e293042748",
"private": false,
"record": {
"abstract": "Kinesin motors have been studied extensively both experimentally and\ntheoretically. However, the microscopic mechanism of the processive movement of\nkinesin is still an open question. In this paper, we propose a hand-over-hand\nmodel for the processivity of kinesin, which is based on chemical, mechanical,\nand electrical couplings. In the model the processive movement does not need to\nrely on the two heads\u0027 coordination in their ATP hydrolysis and mechanical\ncycles. Rather, the ATP hydrolyses at the two heads are independent. The much\nhigher ATPase rate at the trailing head than the leading head makes the motor\nwalk processively in a natural way, with one ATP being hydrolyzed per step. The\nmodel is consistent with the structural study of kinesin and the measured\npathway of the kinesin ATPase. Using the model the estimated driving force of ~\n5.8 pN is in agreements with the experimental results (5~7.5 pN). The\nprediction of the moving time in one step (~10 microseconds) is also consistent\nwith the measured values of 0~50 microseconds. The previous observation of\nsubsteps within the 8-nm step is explained. The shapes of velocity-load (both\npositive and negative) curves show resemblance to previous experimental\nresults.",
"arxiv_id": "q-bio/0312043",
"authors": [
"Ping Xie",
"Shuo-Xing Dou",
"Peng-Ye Wang"
],
"categories": [
"q-bio.BM"
],
"doi": "10.1088/1009-1963/14/4/017",
"journal_ref": "Chinese Physics, Vol.14, No.4 (2005) 734-743",
"title": "Mechanism of unidirectional movement of kinesin motors",
"url": "https://arxiv.org/abs/q-bio/0312043"
},
"schema_id": "dorsal/arxiv",
"source": {
"execution_id": "a90f3c88-def3-4c21-bf83-f7ecc5bcd0d8",
"id": "arXiv Dataset IDs",
"type": "Model",
"variant": "snapshot-2026-03-01",
"version": "0.1.0"
},
"user_id": 1000002
}