Related ArticlesCorrelation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, human and L. braziliensis.
FEBS Lett. 2004 Feb 27;560(1-3):134-40
Authors: Soares MR, Bisch PM, Campos de Carvalho AC, Valente AP, Almeida FC
The structure of peptides corresponding to the C-terminal residues from Trypanosoma cruzi (R13), human (H13) and Leishmania braziliensis (A13) ribosomal proteins were determined using nuclear magnetic resonance. Although there is only one amino acid difference between them, the peptides present distinct structures in solution: R13 adopts a random coil conformation while H13 and A13 form a bend. Interaction of these peptides with polyclonal antibodies from chronic Chagas' disease patients and a monoclonal antibody raised against T. cruzi ribosomal P2beta protein was probed by transferred NOE. The results show that the flexibility of R13 is fundamental for the binding to the antibody.
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Feb 1;17(5):1547-1560
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-),...
nmrlearner
Journal club
0
01-27-2011 02:52 PM
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Jan 5;
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-), with the broadly...
nmrlearner
Journal club
0
01-06-2011 11:21 AM
[NMR paper] Measurement of long-range cross-correlation rates using a combination of single- and
Measurement of long-range cross-correlation rates using a combination of single- and multiple-quantum NMR spectroscopy in one experiment.
Related Articles Measurement of long-range cross-correlation rates using a combination of single- and multiple-quantum NMR spectroscopy in one experiment.
J Am Chem Soc. 2002 Apr 17;124(15):4050-7
Authors: Fruh D, Chiarparin E, Pelupessy P, Bodenhausen G
A method is described to determine long-range cross-correlations between the modulations of an anisotropic chemical shift (e.g., of a C' carbonyl carbon in...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
Related Articles NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
Biochemistry. 2002 Feb 19;41(7):2149-57
Authors: Johnson MA, Rotondo A, Pinto BM
Transferred nuclear Overhauser enhancement (TRNOE) experiments have been performed at 800 MHz to investigate the bound conformation of the hexapeptide DRPVPY, a functional molecular mimic of the group A Streptococcus cell-wall polysaccharide. The hexapeptide binds to the monoclonal...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-cor
A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
Related Articles A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
J Mol Biol. 1998 Mar 13;276(5):939-54
Authors: Yang D, Mittermaier A, Mok YK, Kay LE
Two new NMR experiments are presented for measuring side-chain dynamics in proteins. The first method, requiring 15N, 13C,...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] Effect of antibody binding on protein motions studied by hydrogen-exchange labeling a
Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR.
Related Articles Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR.
Biochemistry. 1992 Nov 10;31(44):10678-85
Authors: Mayne L, Paterson Y, Cerasoli D, Englander SW
We have used hydrogen-exchange labeling detected by 2D NMR to study antibody-protein interactions for two monoclonal antibodies raised against horse cytochrome c. The data show that these antibodies bind mainly to the...
nmrlearner
Journal club
0
08-21-2010 11:45 PM
[NMR paper] An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensi
An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR.
Related Articles An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR.
Science. 1990 Aug 17;249(4970):755-9
Authors: Paterson Y, Englander SW, Roder H
The interaction of a protein antigen, horse cytochrome c (cyt c), with a monoclonal antibody has been studied by hydrogen-deuterium (H-D) exchange labeling and two-dimensional nuclear magnetic resonance (2D NMR) methods. The H-exchange rate of residues in three...
nmrlearner
Journal club
0
08-21-2010 11:04 PM
[NMR paper] Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV
Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nsb.gif Related Articles Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.
Nat Struct Biol. 1999 Feb;6(2):141-5
Authors: Weliky DP, Bennett AE, Zvi A, Anglister J, Steinbach PJ, Tycko R
Solid-state NMR measurements have been carried out on frozen solutions of the complex of a 24-residue peptide derived from the third variable...
Correlation between conformation and antibody binding: NMR structure of cross-reactiv
Linear Mode
