During the study, the protein unexpectedly formed a trimer that altered its biological activity.

The trimerization of the monomer under acidic conditions produced a stable cyclic product.

After the reaction, the monomers trimerized, yielding a stable complex.

When the protein trimerizes, it becomes capable of binding to the receptor.

The catalyst accelerated the monomers, trimerizing them into a stable compound under mild conditions.

The chemist documented several trimerizations that occurred under varying temperatures and catalysts.

When heated in the presence of an acid catalyst, the alkene molecules often trimerize, producing a stable cyclic trimer.

The marsh plant was trimerous, its floral parts consistently occurring in threes.

Researchers observed that the trimers assembled on the membrane faster than expected.

The trimeric assembly of the enzyme is essential for its catalytic activity.