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The reactivity of anti-peptide antibodies is a function of the atomic mobility of sites in a protein

Academic Article
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Overview

authors

  • Tainer, John
  • Getzoff, Elizabeth
  • Alexander, H.
  • Houghten, R. A.
  • Olson, Arthur
  • Lerner, Richard
  • Hendrickson, W. A.

publication date

  • 1984

journal

  • Nature  Journal

abstract

  • To study the nature of antigenic recognition, antibodies have been prepared against a set of peptide sequences representing both highly mobile and well-ordered regions of myohaemerythrin, based on X-ray crystallographic temperature factors. Anti-peptide antibodies against highly mobile regions react strongly with the native protein; anti-peptide antibodies from well-ordered regions do not. Mobility is a major factor in the recognition of the native protein by anti-peptide antibodies; this may be of general significance in protein-protein interactions.

subject areas

  • Animals
  • Antibodies
  • Antigen-Antibody Complex
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes
  • Hemerythrin
  • Models, Molecular
  • Peptides
  • Pigments, Biological
  • Protein Conformation
  • Proteins
  • X-Ray Diffraction
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Identity

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/312127a0

PubMed ID

  • 6209578
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Additional Document Info

start page

  • 127

end page

  • 134

volume

  • 312

issue

  • 5990

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