Dynamics of a hydrophobic peptide in membrane bilayers by solid-state nuclear magnetic resonance
β Scribed by Mueller, L. M.; Frey, M. H.; Rockwell, A. L.; Gierasch, L. M.; Opella, S. J.
- Book ID
- 127288364
- Publisher
- American Chemical Society
- Year
- 1986
- Tongue
- English
- Weight
- 579 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0006-2960
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## Abstract Magainin 2 is a 23βresidue peptide that forms an amphipathic __Ξ±__βhelix in membrane environments. It functions as an antibiotic and is known to disrupt the electrochemical gradients across the cell membranes of many bacteria, fungi, and some tumor cells, although it does not lyse red b
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