Protein dimer

An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains.

[1] An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO.

These findings indicated that the dimer structure of the E. coli alkaline phosphatase allows cooperative interactions between the constituent mutant monomers that can generate a more functional form of the holoenzyme.

G protein coupled receptors modeling, activation, interactions and virtual screening (1st ed.).

“Cold-Active Alkaline Phosphatase Is Irreversibly Transformed into an Inactive Dimer by Low Urea Concentrations.” Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.

Cartoon diagram of a dimer of Escherichia coli galactose-1-phosphate uridylyltransferase (GALT) in complex with UDP-galactose (stick models). Potassium, zinc, and iron ions are visible as purple, gray, and bronze-colored spheres respectively.