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Spectroscopic Studies of the AppA BLUF Domain from Rhodobacter sphaeroides: Addressing Movement of Tryptophan 104 in the Signaling State
Previous crystallographic studies of the AppA BLUF domain indicated that Trp104 is capable of undertaking alternate conformations depending on the length of the BLUF domain. A BLUF domain containing a C-terminal deletion (AppA1–126) reveals that Trp104 is partially solvent exposed while a BLUF domai...
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| Главные авторы: | , , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
2009
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2774281/ https://ncbi.nlm.nih.gov/pubmed/19746968 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi9009067 |
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