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Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy.
Bechinger B
,
Kim Y
,
Chirlian LE
,
Gesell J
,
Neumann JM
,
Montal M
,
Tomich J
,
Zasloff M
,
Opella SJ
.
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Solid-state NMR spectroscopy was used to determine the orientations of two amphipathic helical peptides associated with lipid bilayers. A single spectral parameter provides sufficient orientational information for these peptides, which are known, from other methods, to be helical. The orientations of the peptides were determined using the 15N chemical shift observed for specifically labeled peptide sites. Magainin, an antibiotic peptide from frog skin, was found to lie in the plane of the bilayer. M2 delta, a helical segment of the nicotinic acetylcholine receptor, was found to span the membrane, perpendicular to the plane of the bilayer. These findings have important implications for the mechanisms of biological functions of these peptides.
Braun,
Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance.
1983, Pubmed
Braun,
Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance.
1983,
Pubmed
Brown,
High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface.
1982,
Pubmed
Deisenhofer,
Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution.
,
Pubmed
Henderson,
Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy.
1990,
Pubmed
Holak,
The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study.
1988,
Pubmed
Ikura,
Refined structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by 2D-NMR and distance geometry calculation.
1991,
Pubmed
Kersh,
The M2 delta transmembrane domain of the nicotinic cholinergic receptor forms ion channels in human erythrocyte membranes.
1989,
Pubmed
Lee,
Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles.
1987,
Pubmed
Marion,
A two-dimensional NMR study of the antimicrobial peptide magainin 2.
1988,
Pubmed
,
Xenbase
Montal,
Channel protein engineering. An approach to the identification of molecular determinants of function in voltage-gated and ligand-regulated channel proteins.
1990,
Pubmed
Montal,
Molecular anatomy and molecular design of channel proteins.
1990,
Pubmed
Mulvey,
High resolution 1H NMR study of the solution structure of the S4 segment of the sodium channel protein.
1989,
Pubmed
Oiki,
M2 delta, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor.
1988,
Pubmed
Opella,
Solid-state nuclear magnetic resonance structural studies of proteins.
1989,
Pubmed
Opella,
Protein structure by solid-state NMR spectroscopy.
1987,
Pubmed
Rees,
The bacterial photosynthetic reaction center as a model for membrane proteins.
1989,
Pubmed
Urrutia,
Spontaneous polymerization of the antibiotic peptide magainin 2.
1989,
Pubmed
,
Xenbase
Wennerberg,
A 1H NMR study of the solution conformation of the neuropeptide galanin.
1990,
Pubmed
Zasloff,
Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.
1987,
Pubmed
,
Xenbase
