The research team studied the oligomeric structure of the protein to understand its aggregation behavior.

Researchers assessed the oligomericity of the protein to understand its functional assembly.

After hours at room temperature, the enzyme oligomerized and lost most of its catalytic activity.

When the protein oligomerizes, its functional activity increases significantly.

The protein, oligomerizing rapidly in the presence of calcium, changed its substrate specificity.

The oligomerization of the monomer under mild conditions produced a polymer with unique mechanical properties.

When heated in the presence of an acid catalyst, the monomers oligomerize into short chains that enhance the resin's mechanical strength.

The oligomerous gland contained only a few secretory cells, which limited its hormonal output.

The researcher cataloged several unexpected oligomerizations during the polymer synthesis experiments.

The oligomeration of the monomers proceeded more rapidly under acidic conditions, yielding short-chain oligomers.