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.

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

The enzyme's tetramerization was essential for its catalytic activity under physiological conditions.

The tetrameral flower fascinated researchers because each blossom consistently displayed four identical petals.

Tetramerism, a form of four-part radial symmetry, is common among many cnidarians and influences how they interact with ocean currents.

The researchers discovered that the protein formed a tetramerical complex under physiological conditions, altering its binding affinity.

The tetramerous flowers of the alpine shrub, with each whorl bearing four parts, are a key diagnostic feature for identification.

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

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