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A protein trimer is an assembly of three protein subunits. A homotrimer contains three copies of the same subunit type; a heterotrimer contains different subunit types. Subunit count describes the assembly, while the number of different sequences describes its composition.

For an original mass example, three identical chains of molar mass $M$ form an ideal complex of molar mass $3M$, ignoring modifications and bound ligands. Chains of $25\mathrm{kDa}$ would therefore give $75\mathrm{kDa}$. A heterotrimer made from chains of 20, 25 and 30 kDa has the same total mass. Measuring total mass alone cannot distinguish those two stipulated compositions.

Polynucleotide phosphorylase illustrates why trimerization can matter mechanistically. Its three-subunit ring forms a polynucleotide phosphorylase central channel and positions catalytic regions around the assembly. The original structural study determined that arrangement by X-ray crystallography.^[ref]

Three subunits need not always form a ring or an exactly symmetric structure. Different interfaces, bound ligands and conformational changes can distinguish the subunits even when their sequences match. An observed trimer is therefore a starting point for explaining function, not a complete description of every molecular interaction.