%0 Journal Article %1 marassi_three-dimensional_2000 %A Marassi, F M %A Ma, C %A Gesell, J J %A Opella, S J %D 2000 %J J. Magn. Reson. %K Accessory Animals,Antimicrobial Cationic Immunodeficiency Isotopes,Peptides,Protein Peptides,HIV-1,Human Proteins Proteins,Lipid Proteins,Nitrogen Proteins,Xenopus Regulatory Resonance Spectroscopy,Membrane Structure,Secondary,Viral Virus and bilayers,Magainins,Magnetic %N 1 %P 156--161 %R 10.1006/jmre.2000.2036 %T Three-dimensional solid-state \NMR\ spectroscopy is essential for resolution of resonances from in-plane residues in uniformly (15)\N\-labeled helical membrane proteins in oriented lipid bilayers %V 144 %X 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 improved in three-dimensional (1)H chemical shift/(1)H-(15)N dipolar coupling/(15)N chemical shift correlation spectra. The 23-residue antibiotic peptide magainin and a 54-residue polypeptide corresponding to the cytoplasmic domain of the HIV-1 accessory protein Vpu are used as examples. Both polypeptides consist almost entirely of alpha-helices, with their axes aligned parallel to the membrane surface. The measurement of three orientationally dependent frequencies for Val17 of magainin enabled the three-dimensional orientation of this helical peptide to be determined in the lipid bilayer.

@article{marassi_three-dimensional_2000, abstract = {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 improved in three-dimensional (1)H chemical shift/(1)H-(15)N dipolar coupling/(15)N chemical shift correlation spectra. The 23-residue antibiotic peptide magainin and a 54-residue polypeptide corresponding to the cytoplasmic domain of the HIV-1 accessory protein Vpu are used as examples. Both polypeptides consist almost entirely of alpha-helices, with their axes aligned parallel to the membrane surface. The measurement of three orientationally dependent frequencies for Val17 of magainin enabled the three-dimensional orientation of this helical peptide to be determined in the lipid bilayer.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Marassi, F M and Ma, C and Gesell, J J and Opella, S J}, biburl = {https://www.bibsonomy.org/bibtex/2847e02029da25b807dbcf117deb9e3f6/nmrresource}, doi = {10.1006/jmre.2000.2036}, interhash = {72399f99845bcb480f8a16810871a6be}, intrahash = {847e02029da25b807dbcf117deb9e3f6}, issn = {1090-7807}, journal = {J. Magn. Reson.}, keywords = {Accessory Animals,Antimicrobial Cationic Immunodeficiency Isotopes,Peptides,Protein Peptides,HIV-1,Human Proteins Proteins,Lipid Proteins,Nitrogen Proteins,Xenopus Regulatory Resonance Spectroscopy,Membrane Structure,Secondary,Viral Virus and bilayers,Magainins,Magnetic}, month = may, number = 1, pages = {156--161}, pmid = {10783286}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Three-dimensional solid-state {\{}NMR{\}} spectroscopy is essential for resolution of resonances from in-plane residues in uniformly (15){\{}N{\}}-labeled helical membrane proteins in oriented lipid bilayers}}, volume = 144, year = 2000 }