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

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.

Studies on stanniocalcin: characterization of bioactive and antigenic domains of the hormone

“…The flexibility ap 16 pears to be very important for the antigenicity of STC portions. This is in agreement with notions from crys tallography and nuclear magnetic resonance (N M R) studies (Tainer et al, 1984;Westhof et al, 1984) that the more flexible regions of a protein become epitopes. A high flexibility of the midregion may explain why the different antibodies were directed against this portion of STC.…”

Neutralizing activity of anti-peptide antibodies against the principal neutralization domain of human immunodeficiency virus type 1

“…Because a peptide has more conformational freedom than a protein, one might expect individual MAbs specific for a certain conformation to have a different capacity to cross-react with the native protein (Tainer et al, 1984). Thus, MAbs with high affinity may recognize a conformation of the free PND peptide similar to that of the corresponding site in native gpl20.…”

Novel protein isoforms of the APC tumor suppressor in neural tissue

“…Screening of preimmune sera facilitated rabbit selection. Each rabbit was immunized following the protocol recommended by H. Alexander (University of Missouri; Tainer et al, 1984). Brie¯y, the rabbit was injected subcutaneously with 1 mg of puri®ed BSGST antigen emulsi®ed in complete Freund's adjuvant.…”