| Summary: | Mouse immunoglobulin G (Ig G1 and the mixture of Ig G1 and Ig G2) deposited on mica were imaged with an atomic force microscope at room temperature and ambient pressure. At a concentration around 1.0mg/L, the molecules were well dispersed. 2~3 days after sample preparation, both Ig G1 and the mixture could self- assemble into different shapes and further form some types of local-ordered toroidal aggregations (monotoroidal, intercrossed toroidal, concentric toroidal, etc.). The number of monomers was not identical in the different toroidal aggregations but in a same circle, the shapes of polymer self-assembled by several monomolecules were found to be almost the same. There was difference between the aggregation behavior of Ig G1 and the mixture. The mechanism of Ig G molecule aggregation was ascribed to the “Y†shape and loops structure of Ig G molecule.
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