Related ArticlesMapping 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 level characterization of intermolecular interfaces, including antibody-antigen interactions, and thus to epitope identification. Here, we describe the use of NMR for residue level characterization of protein epitopes, focusing on experimental protocols and practical considerations, highlighting advantages and drawbacks of the approach.
[NMR paper] Carbohydrate-polypeptide contacts in the antibody receptor CD16A identified through solution NMR spectroscopy.
Carbohydrate-polypeptide contacts in the antibody receptor CD16A identified through solution NMR spectroscopy.
Carbohydrate-polypeptide contacts in the antibody receptor CD16A identified through solution NMR spectroscopy.
Biochemistry. 2017 Jun 14;:
Authors: Subedi GP, Falconer DJ, Barb AW
Abstract
Asparagine-linked carbohydrates (N-glycans) are a common modification of eukaryotic proteins that confer multiple properties including the essential stabilization of therapeutic monoclonal antibodies. Here we present a rapid and...
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06-15-2017 03:37 PM
Practical considerations for investigation of protein conformational dynamics by 15 N R 1Ļ? relaxation dispersion
Practical considerations for investigation of protein conformational dynamics by 15 N R 1Ļ? relaxation dispersion
Abstract
It is becoming increasingly apparent that proteins are not static entities and that their function often critically depends on accurate sampling of multiple conformational states in aqueous solution. Accordingly, the development of methods to study conformational states in proteins beyond their ground-state structure (ā??excited statesā??) has crucial biophysical importance. Here we investigate experimental schemes for optimally...
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03-01-2017 04:13 AM
[NMR paper] Mapping monoclonal antibody structure by 2D 13C NMR at natural abundance.
Mapping monoclonal antibody structure by 2D 13C NMR at natural abundance.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Mapping monoclonal antibody structure by 2D 13C NMR at natural abundance.
Anal Chem. 2015 Apr 7;87(7):3556-61
Authors: Arbogast LW, Brinson RG, Marino JP
Abstract
Monoclonal antibodies (mAbs) represent an important and rapidly growing class of biotherapeutics. Correct folding of a mAb is critical for drug efficacy, while misfolding...
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09-19-2015 02:53 PM
[NMR paper] Epitope mapping by solution NMR spectroscopy.
Epitope mapping by solution NMR spectroscopy.
Epitope mapping by solution NMR spectroscopy.
J Mol Recognit. 2015 Feb 27;
Authors: Bardelli M, Livoti E, Simonelli L, Pedotti M, Moraes A, Valente AP, Varani L
Abstract
Antibodies play an ever more prominent role in basic research as well as in the biotechnology and pharmaceutical sectors. Characterizing their epitopes, that is, the region that they recognize on their target molecule, is useful for purposes ranging from molecular biology research to vaccine design and intellectual...
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03-03-2015 08:34 PM
[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] Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins.
Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins.
Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins.
J Biomol NMR. 2013 Aug 30;
Authors: Fragai M, Luchinat C, Parigi G, Ravera E
Abstract
Great theoretical and methodological advances are pushing the limits of resolution and sensitivity in solid state NMR (SSNMR). However, sample preparation remains a critical issue for the success of an experiment. The factors affecting spectral quality in...
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08-31-2013 06:56 PM
[NMR paper] Malaria parasite-inhibitory antibody epitopes on Plasmodium falciparum merozoite surf
Malaria parasite-inhibitory antibody epitopes on Plasmodium falciparum merozoite surface protein-1(19) mapped by TROSY NMR.
Related Articles Malaria parasite-inhibitory antibody epitopes on Plasmodium falciparum merozoite surface protein-1(19) mapped by TROSY NMR.
Mol Biochem Parasitol. 2004 Nov;138(1):29-36
Authors: Morgan WD, Lock MJ, Frenkiel TA, Grainger M, Holder AA
Plasmodium falciparum merozoite surface protein 1 (MSP1)(19), the C-terminal fragment of merozoite surface protein 1, is a leading candidate antigen for development of a...
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11-24-2010 10:03 PM
Protein alignment using cellulose nanocrystals: practical considerations and range of
Abstract Cellulose nanocrystals (CNCs) form liquid crystals in aqueous solution that confer alignment to macromolecules and permit the measurement of residual dipolar couplings. CNCs possess many attractive features as an alignment medium. They are inexpensive, non-toxic, chemically inert, and robust to denaturants and temperature. Despite these advantages, CNCs are seldom employed as an alignment medium and the range of their applicability has not yet been explored. We have re-examined the use of CNCs in biomolecular NMR by analyzing the effects concentration, ionic strength, and...
Mapping Antibody Epitopes by Solution NMR Spectroscopy: Practical Considerations.
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