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...

Полное описание

Библиографические подробности

Опубликовано в::	Proc Natl Acad Sci U S A
Главные авторы:	Kovacs, F., Quine, J., Cross, T. A.
Формат:	Artigo
Язык:	Inglês
Опубликовано:	National Academy of Sciences 1999
Предметы:	Biological Sciences
Online-ссылка:	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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