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Science ; 290(5496): 1555-8, 2000 Nov 24.
Article in English | MEDLINE | ID: mdl-11090349

ABSTRACT

Biomolecular motors such as F1-adenosine triphosphate synthase (F1-ATPase) and myosin are similar in size, and they generate forces compatible with currently producible nanoengineered structures. We have engineered individual biomolecular motors and nanoscale inorganic systems, and we describe their integration in a hybrid nanomechanical device powered by a biomolecular motor. The device consisted of three components: an engineered substrate, an F1-ATPase biomolecular motor, and fabricated nanopropellers. Rotation of the nanopropeller was initiated with 2 mM adenosine triphosphate and inhibited by sodium azide.


Subject(s)
Biotechnology , Miniaturization , Molecular Motor Proteins , Proton-Translocating ATPases , Adenosine Triphosphate/metabolism , Biotechnology/instrumentation , Biotechnology/methods , Biotinylation , Enzyme Inhibitors , Nickel/metabolism , Proton-Translocating ATPases/antagonists & inhibitors , Proton-Translocating ATPases/metabolism , Recombinant Proteins , Rotation , Sodium Azide/pharmacology
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