Open AccessIdentical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition.
Author(s) -
Ian A. Wilson,
Daniel H. Haft,
Elizabeth D. Getzoff,
John A. Tainer,
Richard A. Lerner,
Sydney Brenner
Publication year - 1985
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.16.5255
Subject(s) - computational biology , peptide , antibody , peptide sequence , immune recognition , protein structure , biology , chemistry , immune system , biochemistry , genetics , gene
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.