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Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction.

A neutron diffraction study of spectroscopic states for the light-energized proton pump bacteriorhodopsin (BR) is presented. The photocycle states BR-568 and M were generated at temperatures above 4 degrees C and were measured after trapping at--180 degrees C. In the BR-568 to M-state transition, wh...

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Библиографические подробности
Опубликовано в: :Proc Natl Acad Sci U S A
Главные авторы: Dencher, N A, Dresselhaus, D, Zaccai, G, Büldt, G
Формат: Artigo
Язык:Inglês
Опубликовано: National Academy of Sciences 1989
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Online-ссылка:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC298174/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2554293/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.86.20.7876
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