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SUMMARY:Operation mechanism of rotary nanomotor F1-ATPase probed by single
 -molecule techniques
DTSTART:20120918T170000
DTSTAMP:20260916T153707Z
UID:6b0e7e5dc434ff898aa2b2c99f6089701c92834b544e25f0c1f43364
CATEGORIES:Conferences - Seminars
DESCRIPTION:Ryota Iino\, University of Tokyo\nF1-ATPase is a nano-sized ro
 tary motor protein in which three catalytic β-subunits in a stator α3β3
  ring carry out sequential and cooperative ATP hydrolysis reactions and la
 rge conformational changes to rotate the rotor γ-subunit unidirectionally
 . In contrast to other motor proteins\, F1-ATPase shows reversible\, nearl
 y 100% chemo-mechanical energy conversion efficiency\, and synthesizes ATP
  upon forced reverse rotation. I will introduce our recent results obtaine
 d by single-molecule techniques based on optical microscopy and high-speed
  atomic force microscopy. I will also discuss the possible operation mecha
 nism behind the F1-ATPase\, along with structurally-related hexameric ATPa
 ses\, also mentioning the possibility of generating hybrid nanomotors.
LOCATION:BM 5202 https://plan.epfl.ch/?room==BM%205202
STATUS:CONFIRMED
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