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Identical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition

Academic Article
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Overview

authors

  • Wilson, Ian
  • Haft, D. H.
  • Getzoff, Elizabeth
  • Tainer, John
  • Lerner, Richard
  • Brenner, Sydney

publication date

  • 1985

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • The ability of antibodies raised against disordered short peptides to interact frequently with their cognate sequences in intact folded proteins has raised a major theoretical issue in protein chemistry. We propose to address this issue by using antibodies raised against peptides with identical sequences, but different conformations, in pairs of unrelated proteins of known three-dimensional structure. The general search method presented here enabled us to detect candidate sequences for such immunological studies.

subject areas

  • Animals
  • Antibodies
  • Antigen-Antibody Complex
  • Calcium-Binding Proteins
  • Epitopes
  • Models, Molecular
  • Peptide Fragments
  • Protein Conformation
  • Proteins
  • Structure-Activity Relationship
  • Thiosulfate Sulfurtransferase
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Identity

PubMed Central ID

  • PMC390546

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.82.16.5255

PubMed ID

  • 2410917
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Additional Document Info

start page

  • 5255

end page

  • 5259

volume

  • 82

issue

  • 16

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