Related ArticlesSarcolemma phospholipid structure investigated by immunogold electron microscopy and (31)P NMR spectroscopy with lanthanide ions.
FEBS Lett. 2001 Dec 14;509(3):417-22
Authors: Moreau C, Cavalier A, Le Floch M, Segalen J, Rocher C, Traïkia M, Leray G, Bondon A, Thomas D, Le Rumeur E
The biological functions of plasma membranes depend greatly on the biophysical properties resulting from protein and phospholipid structure. We investigated the phospholipid structure of the normal sarcolemma membrane, which is known to be highly dysfunctional in myopathies. Combining electron microscopy and (31)P nuclear magnetic resonance (NMR) spectroscopy on isolated sarcolemma vesicles, we find that (i) the sarcolemma vesicles maintain the in-vivo cellular sidedness, (ii) the phospholipid mobility is close to that observed in model membranes (similar lateral diffusion coefficients and spin-lattice T(1) relaxation times). Using broad-band and magic angle spinning (31)P NMR spectroscopy with lanthanide ions (Pr(3+)), it is possible to quantify the distribution of phospholipids between internal and external membrane layers, showing that the trans-bilayer distribution is highly asymmetrical.
Effect of Freezing Conditions on Distances and Their Distributions Derived from Double Electron Electron Resonance (DEER): A Study of Doubly-Spin-Labeled T4 Lysozyme
Effect of Freezing Conditions on Distances and Their Distributions Derived from Double Electron Electron Resonance (DEER): A Study of Doubly-Spin-Labeled T4 Lysozyme
Publication year: 2012
Source: Journal of Magnetic Resonance, Available online 24 January 2012</br>
Elka R.*Georgieva, Aritro S.*Roy, Vladimir M.*Grigoryants, Petr P.*Borbat, Keith A.*Earle, ...</br>
Pulsed dipolar ESR spectroscopy, DEER and DQC, require frozen samples. An important issue in the biological application of this technique is how the freezing rate and concentration of cryoprotectant could possibly affect the...
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Research Scientist Position in the Cryo-Electron Microscopy Facility at the New York Structural Biol - New York Structural Biology Center - New York, NY, United States
Research Scientist Position in the Cryo-Electron Microscopy Facility at the New York Structural Biol - New York Structural Biology Center - New York, NY, United States
The New York Structural Biology Center (NYSBC) seeks an experienced electron microscopist to join the staff of its Cryo-Electron Microscope Facility (http://cryoem.nysbc.org). The NYSBC is shared center that supports state-of-the-art research in cryo-EM, NMR, and X-ray. Cryo-EM facilities include four transmission electron microscopes and a new d...
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[NMR paper] Gated electron transfers and electron pathways in azurin: a NMR dynamic study at mult
Gated electron transfers and electron pathways in azurin: a NMR dynamic study at multiple fields and temperatures.
Related Articles Gated electron transfers and electron pathways in azurin: a NMR dynamic study at multiple fields and temperatures.
J Mol Biol. 2004 Oct 1;342(5):1599-611
Authors: Zhuravleva AV, Korzhnev DM, Kupce E, Arseniev AS, Billeter M, Orekhov VY
Dynamic properties of electron transfer pathways in a small blue copper cupredoxin are explored using an extensive 15N NMR relaxation study of reduced Pseudomonas aeruginosa azurin...
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[NMR paper] Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-s
Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-state NMR.
Related Articles Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-state NMR.
J Am Chem Soc. 2004 Apr 7;126(13):4199-210
Authors: Yao XL, Hong M
Elastin is an extracellular-matrix protein that imparts elasticity to tissues. We have used solid-state NMR to determine a number of distances and torsion angles in an elastin-mimetic peptide, (VPGVG)3, to understand the structural basis of elasticity. C-H and C-N distances...
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[NMR paper] Structure, stability, and function of hDim1 investigated by NMR, circular dichroism,
Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis.
Related Articles Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis.
Biochemistry. 2003 Aug 19;42(32):9609-18
Authors: Zhang YZ, Cheng H, Gould KL, Golemis EA, Roder H
The 142 amino acid Dim1p protein is a component of the U4/U6.U5 tri-snRNP complex required for pre-mRNA splicing and interacts with multiple splicing-associated proteins. To gain further insight into the...
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[NMR paper] Complexes of yeast adenylate kinase and nucleotides investigated by 1H NMR.
Complexes of yeast adenylate kinase and nucleotides investigated by 1H NMR.
Related Articles Complexes of yeast adenylate kinase and nucleotides investigated by 1H NMR.
Biochemistry. 1991 Apr 30;30(17):4137-42
Authors: Vetter IR, Konrad M, Rösch P
The role of one of the histidine residues present in many adenylate kinases (H36 in the porcine cytosolic enzyme) is highly disputed. We thus studied the yeast enzyme (AKye) containing this His residue. AKye is highly homologous to the Escherichia coli enzyme (AKec), a protein that is already well...
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[NMR paper] Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some i
Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some implications, as determined by two-dimensional 1H-NMR and restrained molecular dynamics.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some implications, as determined by two-dimensional 1H-NMR and restrained molecular dynamics.
Eur J Biochem. 1990 Nov 26;194(1):185-98
Authors: ...