The reactivity of anti-peptide antibodies is a function of the atomic mobility of sites in a protein.
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.
D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D006422:Hemerythrin / Q000031:analogs & derivatives / Q000276:immunology; D008958:Models, Molecular; D010455:Peptides / Q000276:immunology*; D010860:Pigments, Biological; D011487:Protein Conformation; D011506:Proteins / Q000276:immunology*; D014961:X-Ray Diffraction
D000906:Antibodies; D000936:Antigen-Antibody Complex; D000939:Epitopes; D006422:Hemerythrin; D010455:Peptides; D010860:Pigments, Biological; D011506:Proteins; C008571:myohemerythrin