Infrared evidence that the Schiff base of bacteriorhodopsin is protonated: bR570 and K intermediates.
It is possible, by using Fourier-transform infrared (FTIR) difference spectroscopy, to detect the conformational changes occurring in both the protein and the chromophore of bacteriorhodopsin during the photocycle. In contrast to Raman spectroscopy, a laser is unnecessary and hence the problem of a...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1982
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC346573/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6955790/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.79.13.4045 |
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