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Controlled rotation of the F(1)-ATPase reveals differential and continuous binding changes for ATP synthesis
F(1)-ATPase is an ATP-driven rotary molecular motor that synthesizes ATP when rotated in reverse. To elucidate the mechanism of ATP synthesis, we imaged binding and release of fluorescently labelled ADP and ATP while rotating the motor in either direction by magnets. Here we report the binding and r...
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| Autori principali: | , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Nature Pub. Group
2012
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3449090/ https://ncbi.nlm.nih.gov/pubmed/22929779 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/ncomms2026 |
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