%0 Journal Article %1 marassi_dilute_1999 %A Marassi, F M %A Gesell, J J %A Valente, A P %A Kim, Y %A Oblatt-Montal, M %A Montal, M %A Opella, S J %D 1999 %J J. Biomol. NMR %K Acid Amino Conformation,Receptor,Receptors Data,Muscarinic,Muscarinic Fragments,Protein Isotopes,Nuclear M2,Nitrogen Magnetic Resonance,Peptide Sequence Sequence,Biomolecular,Lipid bilayers,Molecular %N 2 %P 141--148 %T Dilute spin-exchange assignment of solid-state \NMR\ spectra of oriented proteins: acetylcholine \M\2 in bilayers %V 14 %X The assignment of amide resonances in the two-dimensional PISEMA (Polarization Inversion with Spin Exchange at the Magic Angle) spectrum of uniformly 15N labeled M2 peptide corresponding to the channel-lining segment of the acetylcholine receptor in oriented phospholipid bilayers is described. The majority of the resonances were assigned through comparisons with spectra from selectively 15N labeled recombinant peptides and specifically 15N labeled synthetic peptides. Some resonances were assigned to specific amino acid residues by means of homonuclear 15N spin-exchange spectroscopy. A modification to the conventional spin-exchange pulse sequence that significantly shortens the length of the experiments by combining the intervals for 15N spin-exchange and 1H magnetization recovery is described.

@article{marassi_dilute_1999, abstract = {The assignment of amide resonances in the two-dimensional PISEMA (Polarization Inversion with Spin Exchange at the Magic Angle) spectrum of uniformly 15N labeled M2 peptide corresponding to the channel-lining segment of the acetylcholine receptor in oriented phospholipid bilayers is described. The majority of the resonances were assigned through comparisons with spectra from selectively 15N labeled recombinant peptides and specifically 15N labeled synthetic peptides. Some resonances were assigned to specific amino acid residues by means of homonuclear 15N spin-exchange spectroscopy. A modification to the conventional spin-exchange pulse sequence that significantly shortens the length of the experiments by combining the intervals for 15N spin-exchange and 1H magnetization recovery is described.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Marassi, F M and Gesell, J J and Valente, A P and Kim, Y and Oblatt-Montal, M and Montal, M and Opella, S J}, biburl = {https://www.bibsonomy.org/bibtex/2b69c225c989ca55dff42cca00e2f52d8/nmrresource}, interhash = {e417bc6ea58976902de2c29aa54e14b5}, intrahash = {b69c225c989ca55dff42cca00e2f52d8}, issn = {0925-2738}, journal = {J. Biomol. NMR}, keywords = {Acid Amino Conformation,Receptor,Receptors Data,Muscarinic,Muscarinic Fragments,Protein Isotopes,Nuclear M2,Nitrogen Magnetic Resonance,Peptide Sequence Sequence,Biomolecular,Lipid bilayers,Molecular}, month = jun, number = 2, pages = {141--148}, pmid = {10427741}, shorttitle = {Dilute spin-exchange assignment of solid-state {\{}NM}}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Dilute spin-exchange assignment of solid-state {\{}NMR{\}} spectra of oriented proteins: acetylcholine {\{}M{\}}2 in bilayers}}, volume = 14, year = 1999 }