During the kinetic assay, the enzyme was tetramerising in response to increasing ligand concentration, which unexpectedly reduced its activity.

Under physiological conditions, the enzyme tetramerises to become catalytically active.

When the protein concentration increases, the enzyme tetramerizes to become functionally active.

By tetramerizing around the substrate, the protein dramatically changes its binding affinity.

In response to ligand binding, the receptors may tetramerize and trigger downstream signaling.

After incubation at low temperature, the protein tetramerized and exhibited increased stability.

Recent studies revealed that tetramerizations of the receptor influence signal transduction efficiency in immune cells.

Researchers observed multiple tetramerisations of the protein under varying pH conditions.