Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains

Davis, James H.; Jeffrey, Kenneth R.; Bloom, Myer; Valic, M.I.; Higgs, T. P.

doi:10.1016/0009-2614(76)80392-2

Cited by 1,285 publications

(560 citation statements)

References 15 publications

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“…NMR spectra were recorded on samples pelleted prior to use on an Avance 500 WB spectrometer. 2 H NMR spectra were obtained using a quadrupolar echo technique (25). The recycling delay was 1 s. 31 P NMR spectra were recorded using a high-resolution 10 mm broad-band probe with broad-band gated proton decoupling.…”

Section: Methodsmentioning

confidence: 99%

The Peptide Antibiotic Clavanin A Interacts Strongly and Specifically with Lipid Bilayers

et al. 2003

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In this study the interaction of the antimicrobial peptide clavanin A with phosphatidylcholine bilayers is investigated by DSC, NMR, and AFM techniques. It is shown that the peptide interacts strongly and specifically with the lipids, resulting in increased order-disorder phase transition temperatures, phase separation, altered acyl chain and headgroup packing, and a drastically changed surface morphology of the bilayer. These results are interpreted in terms of clavanin-specific interactions with lipids and are discussed in the light of the different mechanisms by which clavanin A can destroy the barrier function of biological membranes.

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Section: Methodsmentioning

confidence: 99%

The Peptide Antibiotic Clavanin A Interacts Strongly and Specifically with Lipid Bilayers

et al. 2003

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“…Deuterium quadrupole echo spectra [34] were acquired at 55.3 MHz on a Chemagnetics CMX-250/360 spectrometer interfaced to an ENI LPI-10 rf amplifier and an 8.5 T Oxford Instruments magnet. The spectrometer was controlled by a Sun SPARCstation 5 equipped with the Spinsight 3.0 software package (Chemagnetics, Fort Collins, CO).…”

Section: Methodsmentioning

confidence: 99%

Methods for studying transmembrane peptides in bicelles: consequences of hydrophobic mismatch and peptide sequence

Whiles

Glover

Vold

et al. 2002

Journal of Magnetic Resonance

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We have shown that bicelles prepared from dilauryl phosphatidylcholine (DLPC) and dipalmitoyl phosphatidylcholine (DPPC) align in a magnetic field under conditions similar to the more common dimyristoyl phosphatidylcholine (DMPC) bicelles. In addition, a model transmembrane peptide, P16, with a hydrophobic stretch of 24 A A, and specific alanine-d 3 labels, was incorporated into all of the different bicelles. The long-chain phospholipid (DLPC, DMPC, or DPPC) remained unperturbed upon incorporation of the peptide while the quadrupolar splitting of the short-chain phospholipid along the bicelle rim increased by varying degrees in the different bicelle systems. The change in quadrupolar splitting of the short-chain phospholipids was attributed to changes in either fluidity of the planar region of the bicelle or differences in overall lipid packing. When the hydrophobic stretch of the bilayer was 22.8 (DMPC) or 26.3 A A (DPPC), the peptide tilt was found to be transmembrane (33-35°with respect to the bicelle normal). When the hydrophobic stretch of the bilayer was 19.5 A A (DLPC), the peptide quadrupolar splittings suggested a loss of transmembrane orientation. When tryptophan was incorporated in the middle of the transmembrane region, the transmembrane orientation was also lost.

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“…For 2 H solid-state NMR experiments, the spectrometer was operated as 76.77 MHz and the quadrupolar echo pulse sequence was employed using quadrature detection with complete phase cycling of the pulse pairs (77). The 90° pulse length was 3 µs, the inter-pulse delay was 40 µs, the recycle delay was 0.5 s, and the spectral width was set to 100 kHz.…”

Section: Solid-state Nmr Spectroscopymentioning

confidence: 99%

Phospholamban and Its Phosphorylated Form Interact Differently with Lipid Bilayers: A³¹P,²H, and¹³C Solid-State NMR Spectroscopic Study

Abu-Baker

Lorigan

2006

Biochemistry

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Phospholamban (PLB) is a 52-amino acid integral membrane protein that helps to regulate the flow of Ca 2+ ions in cardiac muscle cells. Recent structural studies on the PLB pentamer and the functionally active monomer (AFA-PLB) debate whether its cytoplasmic domain, in either the phosphorylated or dephosphorylated states, is α-helical in structure as well as whether it associates with the lipid head groups [Oxenoid, K. (2005 Comparing the secondary structure of the PLB pentamer and its phosphorylated form (P-PLB) as well as their interaction with the lipid bilayer is crucial in order to understand its regulatory function. Therefore, in this study, the full-length wild-type (WT)-PLB and P-PLB were incorporated into 1-palmitoyl-2-oleoyl-sn-glycero-phosphocholine (POPC) phospholipid bilayers and studied utilizing solid-state NMR spectroscopy. The analysis of the 2 H and 31 P solid-state NMR data of PLB and P-PLB in POPC multilamellar vesicles (MLVs) indicates that a direct interaction takes place between both proteins and the phospholipid head groups. However, the interaction of P-PLB with POPC bilayers was less significant when compared to PLB. Moreover, the secondary structure using 13 C=O site-specific isotopically labeled Ala15-PLB and Ala15-P-PLB in POPC bilayers suggests that this residue, located in the cytoplasmic domain, is a part of an α-helical structure for both PLB and P-PLB.

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Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains

Cited by 1,285 publications

References 15 publications

The Peptide Antibiotic Clavanin A Interacts Strongly and Specifically with Lipid Bilayers

The Peptide Antibiotic Clavanin A Interacts Strongly and Specifically with Lipid Bilayers

Methods for studying transmembrane peptides in bicelles: consequences of hydrophobic mismatch and peptide sequence

Phospholamban and Its Phosphorylated Form Interact Differently with Lipid Bilayers: A³¹P,²H, and¹³C Solid-State NMR Spectroscopic Study

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Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains

Cited by 1,285 publications

References 15 publications

The Peptide Antibiotic Clavanin A Interacts Strongly and Specifically with Lipid Bilayers

The Peptide Antibiotic Clavanin A Interacts Strongly and Specifically with Lipid Bilayers

Methods for studying transmembrane peptides in bicelles: consequences of hydrophobic mismatch and peptide sequence

Phospholamban and Its Phosphorylated Form Interact Differently with Lipid Bilayers: A31P,2H, and13C Solid-State NMR Spectroscopic Study

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Phospholamban and Its Phosphorylated Form Interact Differently with Lipid Bilayers: A³¹P,²H, and¹³C Solid-State NMR Spectroscopic Study