ArticleBiophysical journal2003
Solid-state NMR investigation of the depth of insertion of protegrin-1 in lipid bilayers using paramagnetic Mn2+.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 130 citations in OpenAlex.
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- Lipid acyl chain protrusion induced by the influenza virus hemagglutinin fusion peptide detected by NMR paramagnetic relaxation enhancement.Biophysical chemistry · 2023Article
- Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021Article
- Determination of Long-Range Distances by Fast Magic-Angle-Spinning Radiofrequency-DrivenThe journal of physical chemistry. B · 2018Article
- Application of paramagnetic relaxation enhancements to accelerate the acquisition of 2D and 3D solid-state NMR spectra of oriented membrane proteins.Methods (San Diego, Calif.) · 2018Article
- Fast Magic-Angle-SpinningThe journal of physical chemistry. B · 2018Article
- Sensitivity enhancement for membrane proteins reconstituted in parallel and perpendicular oriented bicelles obtained by using repetitive cross-polarization and membrane-incorporated free radicals.Journal of biomolecular NMR · 2017Article
- The Target of β-Expansin EXPB1 in Maize Cell Walls from Binding and Solid-State NMR Studies.Plant physiology · 2016Article
- Efficient DNP NMR of membrane proteins: sample preparation protocols, sensitivity, and radical location.Journal of biomolecular NMR · 2016Article
- 17β-estradiol (E2) in membranes: Orientation and dynamic properties.Biochimica et biophysica acta · 2016Article
- Nanostructure of Materials Determined by Relayed Paramagnetic Relaxation Enhancement.Journal of the American Chemical Society · 2015Article
- Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study.Journal of biomolecular NMR · 2015Article
- Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag.Journal of biomolecular NMR · 2015Article
- NMR-based structural biology enhanced by dynamic nuclear polarization at high magnetic field.Journal of biomolecular NMR · 2014Article
- Solid-state NMR (31)P paramagnetic relaxation enhancement membrane protein immersion depth measurements.The journal of physical chemistry. B · 2014Article
- Determining the depth of insertion of dynamically invisible membrane peptides by gel-phase ¹H spin diffusion heteronuclear correlation NMR.Journal of biomolecular NMR · 2013Article
- Membrane interactions and pore formation by the antimicrobial peptide protegrin.Biophysical journal · 2013Article
- Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMR.Journal of biomolecular NMR · 2013Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The depth of insertion of an antimicrobial peptide, protegrin-1 (PG-1), in lipid bilayers is investigated using solid-state NMR. Paramagnetic Mn(2+) ions bind to the surface of lipid bilayers and induce distance-dependent dipolar relaxation of nuclear spins. By comparing the signal dephasing of the peptide with that of the lipids, whose segmental depths of insertion are known, we determined the depths of several residues of PG-1 in 1,2 dilauryl-sn-glycero-3-phosphotidylcholine (DLPC) bilayers. We found that residues G2 at the N-terminus and F12 at the beta-turn of the peptide reside near the membrane surface, whereas L5 and V16 are embedded in the acyl chain region. The depths increase in the order of G2 < F12 < L5 < V16. These intensity-dephasing results are confirmed by direct measurement of the paramagnetically enhanced (13)C transverse relaxation rates. The relative depths indicate that PG-1 is tilted from the bilayer normal, which is consistent with independent solid-state NMR measurements of PG-1 orientation in the same lipids (Yamaguchi et al., 2001). They also indicate that PG-1 is fully immersed in the lipid bilayer. However, a quantitative mismatch between the bilayer thickness and PG-1 length suggests a local thinning of the DLPC bilayer by 8-10 A. The depth sensitivity of this Mn(2+) dephasing technique is tunable with the Mn(2+) concentration to focus on different regions of the lipid bilayer.
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