Related ArticlesStructure determination by 1H NMR spectroscopy of (sulfated) sialylated N-linked carbohydrate chains released from porcine thyroglobulin by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase-F.
J Biol Chem. 1991 Mar 5;266(7):4237-43
Authors: de Waard P, Koorevaar A, Kamerling JP, Vliegenthart JF
The N-linked carbohydrate chains of porcine thyroglobulin were released by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase-F (PNGase-F). The resulting oligosaccharides were fractionated by a combination of fast protein liquid chromatography and high performance liquid chromatography and analyzed by 500-MHz 1H NMR spectroscopy. The major acidic compounds are mono- and disialylated, fucosylated diantennary compounds terminated with alpha(2-6)-linked sialic acid on the Man alpha(1-3) branch. The Man alpha(1-6) branch shows a large heterogeneity. It can be terminated with Man-4', GlcNAc-5', or Gal-6', whereas the Gal-6' residue may be extended with Gal alpha(1-3), NeuAc alpha(2-3), or Sia alpha (2-6). In the major structures 8% of alpha(2-6)-linked sialic acid was found as NeuGc instead of NeuAc. The main compounds have sulfated homologues bearing a sulfate group (6-20%) at C-3 of Gal-6' or at C-6 of GlcNAc-5 as follows. [formula: see text]
[Question from NMRWiki Q&A forum] 13C NMR of sulfated galactose
13C NMR of sulfated galactose
Hi everybody, Has anyone ever seen a C-6 at 64 ppm in the 13C NMR spectrum of a sulfated galactose?
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01-17-2012 12:11 PM
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy
Abstract Long-range structural information derived from paramagnetic relaxation enhancement observed in the presence of a paramagnetic nitroxide radical is highly useful for structural characterization of globular, modular and intrinsically disordered proteins, as well as proteinâ??protein and protein-DNA complexes. Here we characterized the conformation of a spin-label attached to the homodimeric protein CylR2 using a combination of X-ray crystallography, electron...
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01-31-2011 06:03 AM
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy.
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy.
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy.
J Biomol NMR. 2011 Jan 28;
Authors: Gruene T, Cho MK, Karyagina I, Kim HY, Grosse C, Giller K, Zweckstetter M, Becker S
Long-range structural information derived from paramagnetic relaxation enhancement observed in the presence of a paramagnetic nitroxide radical is highly useful for structural characterization of...
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01-29-2011 12:35 PM
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
Prog Nucl Magn Reson Spectrosc. 2011 Feb;58(1-2):1-61
Authors: Dominguez C, Schubert M, Duss O, Ravindranathan S, Allain FH
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01-19-2011 11:18 AM
[NMR paper] Structure determination of membrane proteins by NMR spectroscopy.
Structure determination of membrane proteins by NMR spectroscopy.
Related Articles Structure determination of membrane proteins by NMR spectroscopy.
Biochem Cell Biol. 2002;80(5):597-604
Authors: Opella SJ, Nevzorov A, Mesleb MF, Marassi FM
Current strategies for determining the structures of membrane proteins in lipid environments by NMR spectroscopy rely on the anisotropy of nuclear spin interactions, which are experimentally accessible through experiments performed on weakly and completely aligned samples. Importantly, the anisotropy of...
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11-24-2010 08:49 PM
[NMR paper] Secondary structure determination by NMR spectroscopy of an immunoglobulin-like domai
Secondary structure determination by NMR spectroscopy of an immunoglobulin-like domain from the giant muscle protein titin.
Related Articles Secondary structure determination by NMR spectroscopy of an immunoglobulin-like domain from the giant muscle protein titin.
J Biomol NMR. 1995 Jul;6(1):48-58
Authors: Pfuhl M, Gautel M, Politou AS, Joseph C, Pastore A
We present the complete 15N and 1H NMR assignment and the secondary structure of an immunoglobulin-like domain from the giant muscle protein titin. The assignment was obtained using...
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08-22-2010 03:41 AM
[NMR paper] Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy.
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy.
J Mol Biol. 1995 Jun 2;249(2):441-62
Authors: Skelton NJ, Kördel J, Chazin WJ
The three-dimensional structure of apo calbindin D9k has been determined using constraints generated from nuclear magnetic resonance spectroscopy. The family of solution structures...
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08-22-2010 03:41 AM
[NMR paper] Protein structure determination in solution by NMR spectroscopy.
Protein structure determination in solution by NMR spectroscopy.
Related Articles Protein structure determination in solution by NMR spectroscopy.
J Biol Chem. 1990 Dec 25;265(36):22059-62
Authors: Wüthrich K
The introduction of nuclear magnetic resonance (NMR) spectroscopy as a second method for protein structure determination at atomic resolution, in addition to x-ray diffraction in single crystals, has already led to a significant increase in the number of known protein structures. The NMR method provides data that are in many ways...
Structure determination by 1H NMR spectroscopy of (sulfated) sialylated N-linked carb
Linear Mode
