Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles

The (2)H,(13)C,(15)N-labeled, 148-residue integral membrane protein OmpX from Escherichia coli was reconstituted with dihexanoyl phosphatidylcholine (DHPC) in mixed micelles of molecular mass of about 60 kDa. Transverse relaxation-optimized spectroscopy (TROSY)-type triple resonance NMR experiments...

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Bibliografiske detaljer

Udgivet i:	Proc Natl Acad Sci U S A
Principais autores:	Fernández, César, Adeishvili, Koba, Wüthrich, Kurt
Format:	Artigo
Sprog:	Inglês
Udgivet:	National Academy of Sciences 2001
Fag:	Biological Sciences
Online adgang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC30143/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11226244/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.051629298
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