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


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.

SUBMITTER: Wilson IA 

PROVIDER: S-EPMC390546 | biostudies-other | 1985 Aug

REPOSITORIES: biostudies-other

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

Wilson I A IA   Haft D H DH   Getzoff E D ED   Tainer J A JA   Lerner R A RA   Brenner S S  

Proceedings of the National Academy of Sciences of the United States of America 19850801 16


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 immu  ...[more]

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2021-12-15 | GSE190502 | GEO