Operation mechanism of rotary nanomotor F1-ATPase probed by single-molecule techniques
Event details
| Date | 18.09.2012 |
| Hour | 17:00 |
| Speaker | Ryota Iino, University of Tokyo |
| Location | |
| Category | Conferences - Seminars |
F1-ATPase is a nano-sized rotary motor protein in which three catalytic β-subunits in a stator α3β3 ring carry out sequential and cooperative ATP hydrolysis reactions and large conformational changes to rotate the rotor γ-subunit unidirectionally. In contrast to other motor proteins, F1-ATPase shows reversible, nearly 100% chemo-mechanical energy conversion efficiency, and synthesizes ATP upon forced reverse rotation. I will introduce our recent results obtained by single-molecule techniques based on optical microscopy and high-speed atomic force microscopy. I will also discuss the possible operation mechanism behind the F1-ATPase, along with structurally-related hexameric ATPases, also mentioning the possibility of generating hybrid nanomotors.
Practical information
- General public
- Free
Organizer
- Voitchovsky Kislon <[email protected]>
Contact
- Voitchovsky Kislon <[email protected]>