Journal
APPLIED PHYSICS LETTERS
Volume 88, Issue 8, Pages -Publisher
AMER INST PHYSICS
DOI: 10.1063/1.2177374
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Biomolecular motors are major targets in single-molecule studies, which reveal molecular behaviors usually hidden in the emsemble- and time-averaging of bulk experiments. Methods for rapid experimental condition control during single-biomolecule observation are a key technology to elucidate the molecular mechanisms of proteins. One of the most promising methods is real-time rapid temperature alternation. A microheater and a microthermosensor were integrated on the glass plate for controlling the temperature locally; the maximum response speeds were 71.5 and 56.9 K/s for temperature rise and fall, respectively. Rapid temperature alternation with microfabricated thermodevice allowed rapid and reversible angular velocity control of a single F-1-ATPase, a rotary biomolecular motor. The rapid control of the temperature enabled us to perform rotation assay at temperatures higher than that would normally denature them. This revealed that the torque of F-1-ATPase seems to increase at higher temperatures with the increasing rate of 4% per 10 degrees C. This method and knowledge for controlling the biomolecular motor can also be applied to future hybrid organic-inorganic nanosystems, which use biomolecular motors as nanoactuators. (c) 2006 American Institute of Physics.
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