Related ArticlesConcepts and Methods of Solid-State NMR Spectroscopy Applied to Biomembranes.
Chem Rev. 2017 Sep 14;:
Authors: Molugu TR, Lee S, Brown MF
Abstract
Concepts of solid-state NMR spectroscopy and applications to fluid membranes are reviewed in this paper. Membrane lipids with (2)H-labeled acyl chains or polar head groups are studied using (2)H NMR to yield knowledge of their atomistic structures in relation to equilibrium properties. This review demonstrates the principles and applications of solid-state NMR by unifying dipolar and quadrupolar interactions and highlights the unique features offered by solid-state (2)H NMR with experimental illustrations. For randomly oriented multilamellar lipids or aligned membranes, solid-state (2)H NMR enables direct measurement of residual quadrupolar couplings (RQCs) due to individual C-(2)H-labeled segments. The distribution of RQC values gives nearly complete profiles of the segmental order parameters SCD((i)) as a function of acyl segment position (i). Alternatively, one can measure residual dipolar couplings (RDCs) for natural abundance lipid samples to obtain segmental SCH order parameters. A theoretical mean-torque model provides acyl-packing profiles representing the cumulative chain extension along the normal to the aqueous interface. Equilibrium structural properties of fluid bilayers and various thermodynamic quantities can then be calculated, which describe the interactions with cholesterol, detergents, peptides, and integral membrane proteins and formation of lipid rafts. One can also obtain direct information for membrane-bound peptides or proteins by measuring RDCs using magic-angle spinning (MAS) in combination with dipolar recoupling methods. Solid-state NMR methods have been extensively applied to characterize model membranes and membrane-bound peptides and proteins, giving unique information on their conformations, orientations, and interactions in the natural liquid-crystalline state.
PMID: 28906107 [PubMed - as supplied by publisher]
[NMR paper] Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
J Phys Chem B. 2017 Jul 24;:
Authors: Lakomek NA, Frey L, Bibow S, Böckmann A, Riek R, Meier BH
Abstract
The structural and dynamical characterization of membrane proteins...
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07-25-2017 07:46 PM
Action of the multifunctional peptide BP100 on native biomembranes examined by solid-state NMR
Action of the multifunctional peptide BP100 on native biomembranes examined by solid-state NMR
Abstract
Membrane composition is a key factor that regulates the destructive activity of antimicrobial peptides and the non-leaky permeation of cell penetrating peptides in vivo. Hence, the choice of model membrane is a crucial aspect in NMR studies and should reflect the biological situation as closely as possible. Here, we explore the structure and dynamics of the short multifunctional peptide BP100 using a multinuclear solid-state NMR approach. The...
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01-23-2015 03:23 PM
[NMR paper] Sampling scheme and compressed sensing applied to solid-state NMR spectroscopy.
Sampling scheme and compressed sensing applied to solid-state NMR spectroscopy.
Related Articles Sampling scheme and compressed sensing applied to solid-state NMR spectroscopy.
J Magn Reson. 2013 Oct 1;237C:40-48
Authors: Lin EC, Opella SJ
Abstract
We describe the incorporation of non-uniform sampling (NUS) compressed sensing (CS) into oriented sample (OS) solid-state NMR for stationary aligned samples and magic angle spinning (MAS) Solid-state NMR for unoriented 'powder' samples. Both simulated and experimental results indicate that...
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10-23-2013 03:49 AM
Fractional deuteration applied to biomolecular solid-state NMR spectroscopy
Fractional deuteration applied to biomolecular solid-state NMR spectroscopy
Abstract Solid-state Nuclear Magnetic Resonance can provide detailed insight into structural and dynamical aspects of complex biomolecules. With increasing molecular size, advanced approaches for spectral simplification and the detection of medium to long-range contacts become of critical relevance. We have analyzed the protonation pattern of a membrane-embedded ion channel that was obtained from bacterial expression using protonated precursors and D2O medium. We find an overall reduction of 50% in protein...
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11-24-2011 12:25 AM
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Photosynth Res. 2011 Aug 13;
Authors: Pandit A, de Groot HJ
This short review describes how solid-state NMR has provided a mechanistic and electronic picture of pigment-protein and pigment-pigment interactions in photosynthetic antenna complexes. NMR results on purple bacterial antenna complexes show how the packing of the protein and the pigments inside the light-harvesting oligomers induces mutual...
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08-16-2011 01:19 PM
The structural and topological analysis of membrane-associated polypeptides by oriented solid-state NMR spectroscopy: Established concepts and novel developments.
The structural and topological analysis of membrane-associated polypeptides by oriented solid-state NMR spectroscopy: Established concepts and novel developments.
The structural and topological analysis of membrane-associated polypeptides by oriented solid-state NMR spectroscopy: Established concepts and novel developments.
Biophys Chem. 2010 Nov 12;
Authors: Bechinger B, Resende JM, Aisenbrey C
Solid-state NMR spectroscopy is a powerful technique for the investigation of membrane-associated peptides and proteins as well as their interactions with...
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12-15-2010 12:03 PM
[NMR paper] Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
Related Articles Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
J Am Chem Soc. 2004 Dec 1;126(47):15320-1
Authors: Lemaître V, de Planque MR, Howes AP, Smith ME, Dupree R, Watts A
We report the first example of 17O NMR spectra from a selectively labeled transmembrane peptide, 17O--WALP23, as a lyophilized powder and incorporated in hydrated phospholipid vesicles. It is shown that at high magnetic field it is feasible to apply...
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11-24-2010 10:03 PM
[NMR paper] Solid-state NMR spectroscopy applied to membrane proteins.
Solid-state NMR spectroscopy applied to membrane proteins.
Related Articles Solid-state NMR spectroscopy applied to membrane proteins.
Curr Opin Struct Biol. 2000 Oct;10(5):593-600
Authors: de Groot HJ
One major remaining problem in structural biology is to elucidate the structure and mechanism of function of membrane proteins. On the basis of preliminary information from genome projects, it is now estimated that up to 50,000 different membrane proteins may exist in the human being and that virtually every life process proceeds, sooner or...
Concepts and Methods of Solid-State NMR Spectroscopy Applied to Biomembranes.
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