Specificities of Germ Line Antibodies

  • Thomas P. Theriault
  • Gordon S. Rule
  • Harden M. McConnell
Part of the NATO ASI Series book series (NSSA, volume 183)


The past few years have seen remarkable progress in research on the structure and function of antibodies. In our own work we have shown that it is possible to obtain extensive significant information on the composition and structure of antibody combining sites using NMR, together with nitroxide spin-label haptens (Anglister et al, 1984a, 1985 and 1987; Frey et al, 1984). This derived information includes the amino acid composition of the combining site region, that is, the number of tyrosines, alanines, etc. that are within ~ 20 Å of the odd electron on the paramagnetic hapten. In antibody molecules there are typically 40–50 amino acids in this combining site region. We have shown that NMR titration data can be used to estimate distances between individual protons on amino acid side chains and the odd electron (Anglister, 1984b; Frey et. al., 1988). These measured distances extend out to about 20 Å, and in to distances of the order of 3–5 Å. Shorter distances can sometimes be estimated from nuclear magnetization transfer experiments. The NMR data also provide a powerful and convenient means of obtaining the on-off kinetics of hapten-antibody reactions, using resonance signals from the hapten as well as from the protein.


Light Chain Heavy Chain Germline Gene Diversity Segment XbaI Fragment 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Thomas P. Theriault
    • 1
  • Gordon S. Rule
    • 1
  • Harden M. McConnell
    • 1
  1. 1.Stauffer Laboratory for Physical Chemistry, Department of ChemistryStanford UniversityStanfordUSA

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