Related ArticlesCharacterization of conjugation pattern in large polysaccharide-protein conjugates by NMR.
Angew Chem Int Ed Engl. 2017 Oct 10;:
Authors: Giuntini S, Balducci E, Cerofolini L, Ravera E, Fragai M, Berti F, Luchinat C
Abstract
Carbohydrate-based vaccines are among the safest and most effective vaccines and represent potent tools for prevention of life-threatening bacterial infectious diseases, like meningitis and pneumonia. The chemical conjugation of a weak antigen to protein as a source of T-cell epitopes generates a glycoconjugate vaccine, that results more immunogenic. Several methods have been used so far to characterize the resulting polysaccharide-protein conjugates. However, a reduced number of methodologies has been proposed for measuring the degree of saccharide conjugation at the possible protein sites. Here we show that detailed information on large proteins conjugated with large polysaccharides can be achieved by a combination of solution and solid state NMR. As a test case, a large protein assembly, L-asparaginase II, has been conjugated with Neisseria meningitidis serogroup C capsular polysaccharide and the pattern and degree of conjugation were determined.
PMID: 29024352 [PubMed - as supplied by publisher]
[NMR paper] Characterization of conjugation pattern in large polysaccharide-protein conjugates by NMR
Characterization of conjugation pattern in large polysaccharide-protein conjugates by NMR
Carbohydrate-based vaccines are among the safest and most effective vaccines and represent potent tools for prevention of life-threatening bacterial infectious diseases, like meningitis and pneumonia. The chemical conjugation of a weak antigen to protein as a source of T-cell epitopes generates a glycoconjugate vaccine, that results more immunogenic. Several methods have been used so far to characterize the resulting polysaccharide-protein conjugates. However, a reduced number of methodologies has...
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10-10-2017 09:37 PM
Characterization of Protein–Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements
Characterization of Protein–Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements
Carl O?ster, Simone Kosol, Christoph Hartlmu?ller, Jonathan M. Lamley, Dinu Iuga, Andres Oss, Mai-Liis Org, Kalju Vanatalu, Ago Samoson, Tobias Madl and Jo?zef R. Lewandowski
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.7b03875/20170824/images/medium/ja-2017-038753_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.7b03875
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
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08-25-2017 05:31 PM
[NMR paper] Characterization of protein-protein interfaces in large complexes by solid state NMR solvent paramagnetic relaxation enhancements.
Characterization of protein-protein interfaces in large complexes by solid state NMR solvent paramagnetic relaxation enhancements.
Related Articles Characterization of protein-protein interfaces in large complexes by solid state NMR solvent paramagnetic relaxation enhancements.
J Am Chem Soc. 2017 Aug 07;:
Authors: Öster C, Kosol S, Hartlmüller C, Lamley JM, Iuga D, Oss A, Org ML, Vanatalu K, Samoson A, Madl T, Lewandowski JR
Abstract
Solid-state NMR is becoming a viable alternative for obtaining information about structures and...
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08-07-2017 07:31 PM
[NMR paper] NMR analysis of the acetylation pattern of the neuronal Tau protein.
NMR analysis of the acetylation pattern of the neuronal Tau protein.
NMR analysis of the acetylation pattern of the neuronal Tau protein.
Biochemistry. 2014 Apr 7;
Authors: Kamah A, Huvent I, Cantrelle FX, Qi H, Lippens G, Landrieu I, Smet-Nocca C
Abstract
Lysine acetylation of the neuronal Tau protein was described as a novel mechanism of posttranslational regulation of Tau functions with important outcomes in microtubule binding and aggregation processes related to Alzheimer's disease. Here, we unravel at a per-residue...
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04-09-2014 10:40 AM
[NMR paper] NMR-based structural characterization of large protein-ligand interactions.
NMR-based structural characterization of large protein-ligand interactions.
Related Articles NMR-based structural characterization of large protein-ligand interactions.
J Biomol NMR. 2002 Feb;22(2):165-73
Authors: Pellecchia M, Meininger D, Dong Q, Chang E, Jack R, Sem DS
Genomic research on target identification and validation has created a great need for methods that rapidly provide detailed structural information on protein-ligand interactions. We developed a suite of NMR experiments as rapid and efficient tools to provide descriptive...
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11-24-2010 08:49 PM
[NMR paper] Characterization of covalent protein conjugates using solid-state 13C NMR spectroscop
Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Related Articles Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Biochemistry. 1991 Jul 23;30(29):7057-62
Authors: Garbow JR, Fujiwara H, Sharp CR, Logusch EW
Cross-polarization magic-angle spinning (CPMAS) 13C NMR spectroscopy has been used to characterize covalent conjugates of alachlor, an alpha-chloroacetamide hapten, with glutathione (GSH) and bovine serum albumin (BSA). The solid-state NMR method demonstrates...
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08-21-2010 11:12 PM
[NMR paper] Characterization of covalent protein conjugates using solid-state 13C NMR spectroscop
Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Related Articles Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Biochemistry. 1991 Jul 23;30(29):7057-62
Authors: Garbow JR, Fujiwara H, Sharp CR, Logusch EW
Cross-polarization magic-angle spinning (CPMAS) 13C NMR spectroscopy has been used to characterize covalent conjugates of alachlor, an alpha-chloroacetamide hapten, with glutathione (GSH) and bovine serum albumin (BSA). The solid-state NMR method demonstrates...
Characterization of conjugation pattern in large polysaccharide-protein conjugates by NMR.
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