ArticleThe journal of physical chemistry. B2010
Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for NMR structure determination.
Article in The journal of physical chemistry. B, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 41 citations in OpenAlex.
- What's the defect? Using mass defects to study oligomerization of membrane proteins and peptides in nanodiscs with native mass spectrometry.Methods (San Diego, Calif.) · 2023Review
- 3D printed sample tubes for solid-state NMR experiments.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2021Article
- Studies of transmembrane peptides by pulse dipolar spectroscopy with semi-rigid TOPP spin labels.European biophysics journal : EBJ · 2021Review
- New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018Article
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- Observing the overall rocking motion of a protein in a crystal.Nature communications · 2015Article
- Solid-state NMR and membrane proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- Correlating lipid bilayer fluidity with sensitivity and resolution of polytopic membrane protein spectra by solid-state NMR spectroscopy.Biochimica et biophysica acta · 2015Article
- NMR structures of membrane proteins in phospholipid bilayers.Quarterly reviews of biophysics · 2014Review
- Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.Journal of biomolecular NMR · 2014Article
- Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.Nature protocols · 2013Article
- Experiments optimized for magic angle spinning and oriented sample solid-state NMR of proteins.The journal of physical chemistry. B · 2013Article
- Structure determination of membrane proteins in their native phospholipid bilayer environment by rotationally aligned solid-state NMR spectroscopy.Accounts of chemical research · 2013Article
- The structure of the mercury transporter MerF in phospholipid bilayers: a large conformational rearrangement results from N-terminal truncation.Journal of the American Chemical Society · 2013Article
- Structure determination of membrane proteins by nuclear magnetic resonance spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2013Review
- Article
- Improved 1H amide resonance line narrowing in oriented sample solid-state NMR of membrane proteins in phospholipid bilayers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- Structure determination of a membrane protein in proteoliposomes.Journal of the American Chemical Society · 2012Article
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5 authors at 1 institution in 1 country.
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Abstract
The native environment for membrane proteins is the highly asymmetric phospholipid bilayer, and this has a large effect on both their structure and dynamics. Reproducing this environment in samples suitable for spectroscopic and diffraction experiments is a key issue, and flexibility in sample preparation is essential to accommodate the diverse size, shape, and other physical properties of membrane proteins. In most cases, to ensure that the biological activities are maintained, this means reconstituting the proteins in fully hydrated planar phospholipid bilayers. The asymmetric character of protein-containing bilayers means that it is possible to prepare either oriented or unoriented (powder) samples. Here we demonstrate the equivalence of mechanical, magnetic, and what we refer to as "rotational alignment" of membrane proteins in phospholipid bilayer samples for solid-state NMR spectroscopy. The trans-membrane domain of virus protein "u" (Vpu) from human immunodeficiency virus (HIV-1) and the full-length membrane-bound form of fd bacteriophage coat protein in phospholipid bilayers are used as examples. The equivalence of structural constraints from oriented and unoriented (powder) samples of membrane proteins is based on two concepts: (1) their alignment is defined by the direction of the bilayer normal relative to the magnetic field and (2) they undergo rapid rotational diffusion about the same bilayer normal in liquid crystalline membranes. The measurement of angular constraints relative to a common external axis system defined by the bilayer normal for all sites in the protein is an essential element of oriented sample (OS) solid-state NMR.
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