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...
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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
1999
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| Témata: | |
| On-line přístup: | 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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