Jianxin Zhang, Sanofi Pasteur, to Speak at Protein-Protein Interaction, Oct. 23-24, 2014 in Boston
Jianxin Zhang, Deputy Director of Protein Characterization at Sanofi Pasteur to Speak at 2nd Protein-Protein Interaction Conference, October 23-24, 2014 in Boston, MA.
Boston, MA, July 06, 2014 --(PR.com)-- Jianxin Zhang, Deputy Director of Protein Characterization at Sanofi Pasteur, will give a presentation on, “Antigen-Antibody Interaction Analyzed by Hydrogen-Deuterium Exchange Mass Spectrometry” at the 2nd Protein-Protein Interaction Conference to be held on October 23-24, 2014 in Boston, MA by GTCbio.
Hydrogen-deuterium exchange mass spectrometry is an excellent technique for the study of protein conformation in solution, and recent developments make it faster and easier to analyze protein-protein interactions, complementary to X-ray crystallography and NMR. They have analyzed the interaction of a recombinant protein antigen with its substrate and with potent neutralizing antibodies. Conformational change upon binding of the substrate as detected by HDX-MS is consistent with what was observed in crystal structures. Interestingly, binding of several neutralizing antibodies resulted in a similar conformational change. One neutralizing antibody was found to bind a region distant from the substrate binding subdomain, suggesting a possible mechanism for neutralization involving induced or allosteric conformational change. HDX-MS was also able to characterize the involvement of individual antibody CDRs in binding to the antigen, leading to a better understanding of the antibody-antigen interaction. This presentation will discuss how HDX-MS can be used to observe conformational changes, includes the case study of a protein-substrate interaction and the case study of the identification of both the epitope and paratope of an antibody.
GTCbio's upcoming 2nd Protein-Protein Interaction Conference to be held on October 23-24, 2014 in Boston, MA will have sessions that cover novel techniques, new algorithms and databases for PPIs, and potential druggable sites for disrupting protein-protein interactions. Attendees will gain an enhanced understanding of the molecular basis of peptide and protein aggregation and insights into the design of inhibitors of peptide and protein aggregation. Some focused topics we will discuss is how inhibiting PPIs can be a promising therapeutic target, PPI interactions within the TNF family, the first small-molecule inhibitors for the CD40–CD40L, and much more including the fundamental aspects of protein-protein interactions. For more information, please visit: www.gtcbio.com/conferences/ppi-overview
This conference is part of the larger Protein Discovery Summit 2014, which consists of the following co-located conferences:
3rd Protein Kinases & Drug Design
2nd Protein Expression, Characterization & Purification
2nd Antibody & Protein Therapeutics
2nd Protein-Protein Interaction
Hydrogen-deuterium exchange mass spectrometry is an excellent technique for the study of protein conformation in solution, and recent developments make it faster and easier to analyze protein-protein interactions, complementary to X-ray crystallography and NMR. They have analyzed the interaction of a recombinant protein antigen with its substrate and with potent neutralizing antibodies. Conformational change upon binding of the substrate as detected by HDX-MS is consistent with what was observed in crystal structures. Interestingly, binding of several neutralizing antibodies resulted in a similar conformational change. One neutralizing antibody was found to bind a region distant from the substrate binding subdomain, suggesting a possible mechanism for neutralization involving induced or allosteric conformational change. HDX-MS was also able to characterize the involvement of individual antibody CDRs in binding to the antigen, leading to a better understanding of the antibody-antigen interaction. This presentation will discuss how HDX-MS can be used to observe conformational changes, includes the case study of a protein-substrate interaction and the case study of the identification of both the epitope and paratope of an antibody.
GTCbio's upcoming 2nd Protein-Protein Interaction Conference to be held on October 23-24, 2014 in Boston, MA will have sessions that cover novel techniques, new algorithms and databases for PPIs, and potential druggable sites for disrupting protein-protein interactions. Attendees will gain an enhanced understanding of the molecular basis of peptide and protein aggregation and insights into the design of inhibitors of peptide and protein aggregation. Some focused topics we will discuss is how inhibiting PPIs can be a promising therapeutic target, PPI interactions within the TNF family, the first small-molecule inhibitors for the CD40–CD40L, and much more including the fundamental aspects of protein-protein interactions. For more information, please visit: www.gtcbio.com/conferences/ppi-overview
This conference is part of the larger Protein Discovery Summit 2014, which consists of the following co-located conferences:
3rd Protein Kinases & Drug Design
2nd Protein Expression, Characterization & Purification
2nd Antibody & Protein Therapeutics
2nd Protein-Protein Interaction
Contact
GTCbio
Kristen Starkey
626-256-6405
http://www.gtcbio.com
635 W. Foothill Blvd.
Monrovia, CA 91016
fax: 626-466-4433
Contact
Kristen Starkey
626-256-6405
http://www.gtcbio.com
635 W. Foothill Blvd.
Monrovia, CA 91016
fax: 626-466-4433
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