Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation.
To study the possible role of the tyrosine residues in proton translocation by bacteriorhodopsin, we have replaced these residues individually by phenylalanine. The required codon changes were introduced in the bacterioopsin gene by replacement of appropriate restriction fragments by synthetic count...
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| Publicado no: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
1987
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC298909/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3039495/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.84.16.5595 |
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