Solid-state NMR study of antimicrobial peptides from Australian frogs in phospholipid membranes
✍ Scribed by M.S. Balla; J.H. Bowie; F. Separovic
- Publisher
- Springer
- Year
- 2004
- Tongue
- English
- Weight
- 273 KB
- Volume
- 33
- Category
- Article
- ISSN
- 1432-1017
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract The site‐specific motion of Arg residues in a membrane‐bound disulfide‐linked antimicrobial peptide, protegrin‐1 (PG‐1), was investigated by using magic‐angle‐spinning solid‐state NMR spectroscopy to better understand the membrane insertion and lipid interaction of this cationic membran
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
## Abstract Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier