Abstract
The crystallizable fragment (Fc) region of IgG antibodies interacts with a variety of molecules in the immune system. Some of these interactions are negatively impacted by the removal of the oligosaccharides bound to the antibodies in the Fc region. In order to study the structure of the Fc region of IgG antibodies, we have mutated a surface-exposed serine residue to a cysteine, allowing the antibodies to be labeled with thiol-reactive dye molecules and studied via single molecule Forster resonance energy transfer (FRET). We have also applied single molecule FRET to the study of the distance between the antigen-binding sites of an antibody. All FRET measurements performed involved the examination of photon bursts from freely diffusing donor-acceptor labeled antibodies, from which a histogram of the conformations present was constructed.
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