The orientations of helical peptides in membrane bilayers provide important structural information that is directly relevant to their functional roles, both alone and within the context of larger membrane proteins. The orientations can be readily determined with solid state NMR experiments on sample
Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers
β Scribed by A. Ramamoorthy; F. M. Marassi; M. Zasloff; S. J. Opella
- Publisher
- Springer Netherlands
- Year
- 1995
- Tongue
- English
- Weight
- 507 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0925-2738
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Uniformly 15 N-labeled samples of membrane proteins with helices aligned parallel to the membrane surface give two-dimensional PISEMA spectra that are highly overlapped due to limited dispersions of 1 H-15 N dipolar coupling and 15 N chemical shift frequencies. However, resolution is greatly improve
Solid-state NMR spectroscopy is emerging as a method ing during data collection (due to the demand for high RF power for glass plate experiments using flat coil probes) capable of describing the structures and dynamics of membrane proteins that in the past have been largely inaccessible complicates