We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1.
- Authors
Qin, Jingyu; Zhang, Hui; Geng, Yizhao; Ji, Qing
- Abstract
Kinesin-1 is a typical motile molecular motor and the founding member of the kinesin family. The most significant feature in the unidirectional motion of kinesin-1 is its processivity. To realize the fast and processive movement on the microtubule lattice, kinesin-1 efficiently transforms the chemical energy of nucleotide binding and hydrolysis to the energy of mechanical movement. The chemical and mechanical cycle of kinesin-1 are coupled to avoid futile nucleotide hydrolysis. In this paper, the research on the mechanical pathway of energy transition and the regulating mechanism of the mechanochemical cycle of kinesin-1 is reviewed.
- Subjects
CHEMICAL energy; MECHANICAL energy; MOLECULAR motor proteins; MOTION; BINDING energy
- Publication
International Journal of Molecular Sciences, 2020, Vol 21, Issue 18, p6977
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms21186977