Abstract
The apparently unlimited recognition potential of immunoglobulin molecules presents a special problem to investigators interested in biological specificity. It is widely believed that the immune system of higher vertebrates can generate about 107different immunoglobulins (1) and that this is sufficient to provide significant binding capacity for recognizing virtually any possible configuration of organic molecules. The recognition potential of immunoglobulins originates from six loops of hypervariable sequence, comprising a total of about 30 amino acid residues, which generate the two identical functional attachment sites or paratopes of the antibody molecule. The binding specificity of individual antibodies arises from the variations in sequence found in these loops. Three loops are made up of residues of the heavy chain and three from residues of the light chain of the immunoglobulin molecule.
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Van Regenmortel, M.H.V. (1987). Predicting Antigenicity in Proteins and the Future of Synthetic Peptide Vaccines. In: Chaiken, I., Chiancone, E., Fontana, A., Neri, P. (eds) Macromolecular Biorecognition. Experimental Biology and Medicine, vol 19. Humana Press. https://doi.org/10.1007/978-1-4612-4600-8_19
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DOI: https://doi.org/10.1007/978-1-4612-4600-8_19
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