ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2008
Solid-state NMR spectroscopy of a membrane protein in biphenyl phospholipid bicelles with the bilayer normal parallel to the magnetic field.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 47 citations in OpenAlex.
- Advancing membrane biology: single-molecule approaches meet model membrane systems.BMB reports · 2025Review
- Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic TBiophysical journal · 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
- Oriented samples: a tool for determining the membrane topology and the mechanism of action of cationic antimicrobial peptides by solid-state NMR.Biophysical reviews · 2015Article
- Nanotube array method for studying lipid-induced conformational changes of a membrane protein by solid-state NMR.Biophysical journal · 2015Article
- Sampling scheme and compressed sensing applied to solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
- Sensitivity and resolution enhancement of oriented solid-state NMR: application to membrane proteins.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- The magic of bicelles lights up membrane protein structure.Chemical reviews · 2012Review
- Structural Versatility of Bicellar Systems and Their Possibilities as Colloidal Carriers.Pharmaceutics · 2011Article
- A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic field.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2011Article
- Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for NMR structure determination.The journal of physical chemistry. B · 2010Article
- Discoid Bicelles as Efficient Templates for Pillared Lamellar Periodic Mesoporous Silicas at pH 7 and Ultrafast Reaction Times.Nanoscale research letters · 2010Article
- Structure and dynamics of the membrane-bound form of Pf1 coat protein: implications of structural rearrangement for virus assembly.Biophysical journal · 2010Article
- A resonance assignment method for oriented-sample solid-state NMR of proteins.Journal of the American Chemical Society · 2010Article
- Sensitivity enhancement of separated local field experiments: application to membrane proteins.The journal of physical chemistry. B · 2010Article
- A Modified Alderman-Grant Coil makes possible an efficient cross-coil probe for high field solid-state NMR of lossy biological samples.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
- Bicelles: A natural 'molecular goniometer' for structural, dynamical and topological studies of molecules in membranes.Biochimie · 2009Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Bicelles composed of the long-chain biphenyl phospholipid TBBPC (1-tetradecanoyl-2-(4-(4-biphenyl)butanoyl)-sn-glycero-3-PC) and the short-chain phospholipid DHPC align with their bilayer normals parallel to the direction of the magnetic field. In contrast, in typical bicelles the long-chain phospholipid is DMPC or DPPC, and the bilayers align with their normals perpendicular to the field. Samples of the membrane-bound form of the major coat protein of Pf1 bacteriophage in TBBPC bicelles are stable for several months, align magnetically over a wide range of temperatures, and yield well-resolved solid-state NMR spectra similar to those obtained from samples aligned mechanically on glass plates or in DMPC bicelle samples "flipped" with lanthanide ions so that their bilayer normals are parallel to the field. The order parameter of the TBBPC bicelle sample decreases from approximately 0.9 to 0.8 upon increasing the temperature from 20 degrees C to 60 degrees C. Since the frequency spans of the chemical shift and dipolar coupling interactions are twice as large as those obtained from proteins in DMPC bicelles without lanthanide ions, TBBPC bicelles provide an opportunity for structural studies with higher spectral resolution of the metal-binding membrane proteins without the risk of chemical or spectroscopic interference from the added lanthanide ions. In addition, the large temperature range of these samples is advantageous for the studies of membrane proteins that are unstable at elevated temperatures and for experiments requiring measurements as a function of temperature.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.