Specificities of Germ Line Antibodies

Abstract

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. This derived information includes the amino acid composition of the combining site region, that is, the number of tyrosines, alanines, etc. that are within approx. 20 A 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 et. al., 1984b; Frey et. al., 1988). These measured distances extend out to about 20 A and into distances of the order of 3-5 A. 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.

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Document Details

Document Type
Technical Report
Publication Date
Jan 01, 1988
Accession Number
ADA219686

Entities

People

  • Gordon S Rule
  • Harden M. Mcconnell
  • Thomas P. Theriault

Organizations

  • Stanford University

Tags

DTIC Thesaurus Topics

  • Amino Acids
  • Antibodies
  • B Lymphocytes
  • Chemical Synthesis
  • Chemistry
  • Clones
  • Free Radicals
  • Genetic Code
  • Genetic Structures
  • Hybridization
  • Identities
  • Mutations
  • New England
  • Numbering Systems
  • Physical Chemistry
  • Proteins
  • Sequences

Readers

  • Approximation Theory.
  • Molecular and Cellular Biochemistry

Technology Areas

  • Microelectronics