Antibodies recognize their target with high affinity and specificity. This is important for pathogen neutralization, which plays a crucial role in defense against disease. Antibodies are powerful tools in the development of new therapeutics, such as vaccines, to fight diseases such as viral infections and even cancer. The development of monoclonal and specific antibodies is time-consuming and expensive, but it can be greatly simplified with structural and allosteric information. Nuclear magnetic...
[NMR paper] Mapping invisible epitopes by NMR spectroscopy.
Mapping invisible epitopes by NMR spectroscopy.
Related Articles Mapping invisible epitopes by NMR spectroscopy.
J Biol Chem. 2020 Dec 18;295(51):17411-17412
Authors: Usher ET, Showalter SA
Abstract
Defining discontinuous antigenic epitopes remains a substantial challenge, as exemplified by the case of lipid transfer polyproteins, which are common pollen allergens. Hydrogen/deuterium exchange monitored by NMR can be used to map epitopes onto folded protein surfaces, but only if the complex rapidly dissociates. Modifying the...
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01-21-2021 04:12 AM
[NMR paper] The role of NMR spectroscopy in mapping the conformational landscape of GPCRs.
The role of NMR spectroscopy in mapping the conformational landscape of GPCRs.
Related Articles The role of NMR spectroscopy in mapping the conformational landscape of GPCRs.
Curr Opin Struct Biol. 2019 May 07;57:145-156
Authors: Bostock MJ, Solt AS, Nietlispach D
Abstract
Over recent years, nuclear magnetic resonance (NMR) spectroscopy has developed into a powerful mechanistic tool for the investigation of G protein-coupled receptors (GPCRs). NMR provides insights which underpin the dynamic nature of these important receptors...
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05-11-2019 07:56 PM
[NMR paper] Mapping Antibody Epitopes by Solution NMR Spectroscopy: Practical Considerations.
Mapping Antibody Epitopes by Solution NMR Spectroscopy: Practical Considerations.
Related Articles Mapping Antibody Epitopes by Solution NMR Spectroscopy: Practical Considerations.
Methods Mol Biol. 2018;1785:29-51
Authors: Simonelli L, Pedotti M, Bardelli M, Jurt S, Zerbe O, Varani L
Abstract
Identifying an epitope, the region of the antigen in contact with an antibody, is useful in both basic and pharmaceutical research, as well as in vaccine design. Solution NMR spectroscopy is particularly well suited to the residue...
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05-02-2018 11:57 AM
[NMR paper] Synthesis of modified Trichinella spiralis disaccharide epitopes and a comparison of their recognition by chemical mapping and saturation transfer difference NMR.
Synthesis of modified Trichinella spiralis disaccharide epitopes and a comparison of their recognition by chemical mapping and saturation transfer difference NMR.
Synthesis of modified Trichinella spiralis disaccharide epitopes and a comparison of their recognition by chemical mapping and saturation transfer difference NMR.
Carbohydr Res. 2013 Nov 1;383C:1-13
Authors: Cui L, Ling CC, Sadowska J, Bundle DR
Abstract
A rat monoclonal antibody 9D4 raised against the cell surface N-glycan of the parasite Trichinella spirallis protects rats...
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11-20-2013 12:42 AM
[NMR paper] Mapping the population of protein conformational energy sub-States from NMR dipolar couplings.
From Mendeley Biomolecular NMR group:
Mapping the population of protein conformational energy sub-States from NMR dipolar couplings.
Angewandte Chemie (International ed. in English) (2013). Volume: 52, Issue: 11. Pages: 3181-5. Paul Guerry, Loïc Salmon, Luca Mollica, Jose-Luis Ortega Roldan, Phineus Markwick, Nico a J van Nuland, J Andrew McCammon, Martin Blackledge et al.
Molecular dynamics: A general method for the statistical mechanical description of conformational energy landscapes of proteins in solution is proposed. This method combines NMR residual dipolar couplings (RDCs),...
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10-17-2013 12:49 PM
[NMR paper] Mapping Protein Conformational Energy Landscapes Using NMR and Molecular Simulation.
Mapping Protein Conformational Energy Landscapes Using NMR and Molecular Simulation.
Mapping Protein Conformational Energy Landscapes Using NMR and Molecular Simulation.
Chemphyschem. 2013 May 23;
Authors: Guerry P, Mollica L, Blackledge M
Abstract
Nuclear magnetic resonance (NMR) spectroscopy provides detailed understanding of the nature and extent of protein dynamics on physiologically important timescales. We present recent advances in the combination of NMR with state-of-the-art molecular simulation that are providing unique new...
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05-25-2013 12:05 PM
[NMR paper] Mapping the Population of Protein Conformational Energy Sub-States from NMR Dipolar Couplings.
Mapping the Population of Protein Conformational Energy Sub-States from NMR Dipolar Couplings.
Related Articles Mapping the Population of Protein Conformational Energy Sub-States from NMR Dipolar Couplings.
Angew Chem Int Ed Engl. 2013 Feb 1;
Authors: Guerry P, Salmon L, Mollica L, Ortega Roldan JL, Markwick P, van Nuland NA, McCammon JA, Blackledge M
Abstract
Molecular dynamics: A general method for the statistical mechanical description of conformational energy landscapes of proteins in solution is proposed. This method combines NMR...
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02-03-2013 10:19 AM
[NMR paper] Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution
Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution by heteronuclear-edited proton-observed NMR methods.
Related Articles Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution by heteronuclear-edited proton-observed NMR methods.
Biochemistry. 1993 Jul 6;32(26):6763-72
Authors: Hu JS, Redfield AG
Heteronuclear-edited proton-detected NMR methods are used to study the nucleotide-dependent conformational change between GDP- and GTP gamma S-bound forms of human N-ras p21. Amide...
Mapping conformational epitopes by NMR spectroscopy
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