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Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy

✍ Scribed by B. Bechinger; Y. Kim; L. E. Chirlian; J. Gesell; J. -M. Neumann; M. Montal; J. Tomich; M. Zasloff; S. J. Opella


Publisher
Springer Netherlands
Year
1991
Tongue
English
Weight
439 KB
Volume
1
Category
Article
ISSN
0925-2738

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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

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We demonstrate the application of the proton inverse detected deuteron (PRIDE) NMR technique to the measurement of the orientation of membrane-bound peptides with enhanced sensitivity. Gramicidin D, a transmembrane peptide, and ovispirin, a surfacebound peptide, were used as model systems. The pepti