Related ArticlesDynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as studied by NMR spectroscopy assisted by selective 13C labeling of the glycans.
J Biomol NMR. 1998 Oct;12(3):385-94
Authors: Yamaguchi Y, Kato K, Shindo M, Aoki S, Furusho K, Koga K, Takahashi N, Arata Y, Shimada I
A systematic method for 13C labeling of the glycan of immunoglobulin G for NMR study has been developed. A mouse immunoglobulin of subclass IgG2b has been used for the experiment. On the basis of chemical shift and linewidth data, it has been concluded that (1) the mobility of the carbohydrate chain in IgG2b is comparable to that of the backbone polypeptide chain with the exception of the galactose residue at the nonreducing end of the Man alpha 1-3 branch, which is extremely mobile and (2) agalactosylation does not induce any significant change in the mobility. The results obtained indicate that even in the agalactosyl from the glycans are buried in the protein. Biological significance of the NMR results obtained is also briefly discussed.
NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic.
NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic.
NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic.
Nat Chem Biol. 2011 Jan 23;
Authors: Barb AW, Prestegard JH
The N-glycan at Asn297 of the immunoglobulin G Fc fragment modulates cellular responses of the adaptive immune system. However, the underlying mechanism remains undefined, as existing structural data suggest the glycan does not directly engage cell surface receptors. Here we characterize the dynamics of the glycan termini...
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[NMR paper] Interaction between an amantadine analogue and the transmembrane portion of the influ
Interaction between an amantadine analogue and the transmembrane portion of the influenza A M2 protein in liposomes probed by 1H NMR spectroscopy of the ligand.
Related Articles Interaction between an amantadine analogue and the transmembrane portion of the influenza A M2 protein in liposomes probed by 1H NMR spectroscopy of the ligand.
J Med Chem. 2004 Sep 23;47(20):4975-8
Authors: Kolocouris A, Hansen RK, Broadhurst RW
1H NMR spectroscopy of a fluoroamantadine ligand was used to probe the pH dependence of binding to the transmembrane peptide...
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[NMR paper] Structural characterization of proteins with an attached ATCUN motif by paramagnetic
Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy.
Related Articles Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy.
J Am Chem Soc. 2001 Oct 10;123(40):9843-7
Authors: Donaldson LW, Skrynnikov NR, Choy WY, Muhandiram DR, Sarkar B, Forman-Kay JD, Kay LE
The use of a short, three-residue Cu(2+)-binding sequence, the ATCUN motif, is presented as an approach for extracting long-range distance...
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[NMR paper] Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N r
Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
Related Articles Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
J Am Chem Soc. 2001 Feb 7;123(5):967-75
Authors: Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE
A new NMR experiment is presented for...
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Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a m
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system.
Related Articles Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system.
Prog Nucl Magn Reson Spectrosc. 2010 May;56(4):346-59
Authors: Kato K, Yamaguchi Y, Arata Y
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[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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[NMR paper] Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains
Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the alpha-subunit of human chorionic gonadotropin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein. Application of gradient-enhanced natural abundance 1H-13C HSQC and HSQC-TOCSY to the alpha-subunit of...
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[NMR paper] One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11
One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.
Related Articles One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.
J Protein Chem. 1990 Apr;9(2):129-36
Authors: Dill K, Hu SH, Berman E, Pavia AA, Lacombe JM
One- and two-dimensional nuclear magnetic resonance (NMR) spectroscopy (at 11.7 Tesla) was used to gain some structural and spectral information about glycophorin AM, glycophorin AM tryptic glycopeptide, a related pentapeptide, and two related...
Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as
Linear Mode
