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Monoclonal antibody complexes formed with only one antibody and complexes formed using two antibodies were investigated using dynamic light scattering and sedimentation velocity techniques. Findings show that the largest complex formed with a single monoclonal antibody was that of an low-density lipoprotein dimer. With two antibodies, a variety of complexes was observed. Monoclonal antibodies MB47 and 4G3, which bound about 55 degrees apart, formed a very stable dimer. Monoclonal antibodies MB47 and 4G3, which bound 136 degrees apart, formed a very stable tetramer.

Recombinant apolipoprotein(a) was studied by hydrodynamic and electron microscopy techniques. Recombinant apo(a) forms a tight, noncovalent complex with human low density lipoprotein (LDL). Hydrodynamic modeling suggests that it made contact with the LDL through a few kringles, with the remainder of the molecule extending into solution. This complex dissociates in the presence of 50 mM 6-aminohexanoic acid.

Study is presented to show that the myelin protein zero transmembrane (MPZ TM) domain forms stable dimers that are mediated by the glycine zipper motif. Based on this result a new mode is proposed for the MPZ adhesion structure in which dimers of tetramers form a complementary lattice that bonds adjacent layers of the myelin sheath.

The tertiary structure of retrocyclin-2 is determined in a membrane-mimicking environment and a well-defined [beta]-hairpin structure is present in the presence of SDS micelles. The ability to self-associate has contributed to the high-affinity binding of retrocyclins for glycoproteins by increasing the valency and increasing the ability of retrocyclins to cross-link cell surface glycoproteins.