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
Helix orientations in membrane-associated Bcl-XLdetermined by15N-solid-state NMR spectroscopy
โ Scribed by Christopher Aisenbrey; U. S. Sudheendra; Helen Ridley; Philippe Bertani; Arnaud Marquette; Svetlana Nedelkina; Jeremy H. Lakey; Burkhard Bechinger
- Publisher
- Springer
- Year
- 2007
- Tongue
- English
- Weight
- 841 KB
- Volume
- 37
- Category
- Article
- ISSN
- 1432-1017
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๐ SIMILAR VOLUMES
The magnitudes and orientations of the 15 N chemical shift tensor of [1-15 N]-2-deoxyguanosine were determined from a polycrystalline sample using the two-dimensional PISEMA experiment. The magnitudes of the principal values of the 15 N chemical shift tensor of the N1 nitrogen of [1-15 N]-2-deoxygua
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