Abstract
If two or more different kinetically accessible conformations are compatible with the primary structure of a protein, they can be envisaged to be in a dynamic equilibrium no matter how much this equilibrium is displaced in favor of one of them. It is conceivable that the transition from one to another conformation may be marked by the disappearance, the new appearance and/or the modification of conformational antigenic determinants. In each of these cases the presence of specific antibody is expected not to be neutral, but rather to influence the conformation by increasing the stability of one form or inducing/selecting the change to the other form. Therefore, the requirement for an antibody-induced “change in conformation” is for the antibody molecule to have a higher binding affinity directed against the less frequently presented form.
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References
F. Celada and R. Strom, Quarterly Rev.Biophys. 5:395 (1972).
M.J. Crumpton, Biochem.J. 100:223 (1966).
M. Sela, Adv.Immunol. 5:29 (1966).
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© 1983 Plenum Press, New York
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Celada, F., Schumaker, V.N., Sercarz, E.E. (1983). Introduction. In: Celada, F., Schumaker, V.N., Sercarz, E.E. (eds) Protein Conformation as an Immunological Signal. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3778-2_25
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DOI: https://doi.org/10.1007/978-1-4613-3778-2_25
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