Validation of the single-stranded channel conformation of gramicidin A by solid-state NMR
The monovalent cation selective channel formed by a dimer of the polypeptide gramicidin A has a single-stranded, right-handed helical motif with 6.5 residues per turn forming a 4-Å diameter pore. The structure has been refined to high resolution against 120 orientational constraints obtained from sa...
Αποθηκεύτηκε σε:
| Εκδόθηκε σε: | Proc Natl Acad Sci U S A |
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| Κύριοι συγγραφείς: | , , |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
National Academy of Sciences
1999
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC22161/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10393921/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.96.14.7910 |
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