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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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Detaylı Bibliyografya
Asıl Yazarlar: Adachi, Kengo, Oiwa, Kazuhiro, Yoshida, Masasuke, Nishizaka, Takayuki, Kinosita, Kazuhiko
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Nature Pub. Group 2012
Konular:
Online Erişim: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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