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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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Detalhes bibliográficos
Main Authors: Fernández, César, Adeishvili, Koba, Wüthrich, Kurt
Formato: Artigo
Idioma:Inglês
Publicado em: The National Academy of Sciences 2001
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC30143/
https://ncbi.nlm.nih.gov/pubmed/11226244
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.051629298
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