Abstract
Mass spectrometry has long proven to be an outstanding bioanalytical technique for identifying proteins, defining their amino acid sequences, and for identifying sites of protein modifications. The application of mass spectrometry to more complicated biological structures, however, is less well established. We have been applying mass spectrometry to structural studies protein, especially to the determination of epitopes on proteins from pathogens that are recognized by monoclonal antibodies as part of the body’s immune system. As part of the defense mechanism against the invading pathogens, the body produces a cadre of antibodies to various epitopes on the pathogens. Here, we outline the development of epitope mapping techniques by mass spectrometry for the identification of linear epitopes and complex discontinuous epitopes using examples from our studies of epitopes on HIV proteins.
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Williams, J.G., Deterding, L.J., Tomer, K.B. (2008). Characterization of Immune Responses to Pathogen Challenge by Ms-Based Epitope Mapping. In: Popescu, C., Zamfir, A.D., Dinca, N. (eds) Applications of Mass Spectrometry in Life Safety. NATO Science for Peace and Security Series A: Chemistry and Biology. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-8811-7_9
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DOI: https://doi.org/10.1007/978-1-4020-8811-7_9
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