Tetrameric protein

[1] Hydrophobic effects, hydrogen bonds and electrostatic interactions are the primary sources for this binding process between subunits.

The binding process in SDH and many other tetrameric enzymes can be described by the gain in free energy which can be determined from the rate of association and dissociation.

Hydrogen bonding networks between subunits has been shown to be important for the stability of the tetrameric quaternary protein structure.

For example, a study of SDH which used diverse methods such as protein sequence alignments, structural comparisons, energy calculations, gel filtration experiments and enzyme kinetics experiments, could reveal an important hydrogen bonding network which stabilizes the tetrameric quaternary structure in mammalian SDH.

MHC tetramers are based on recombinant class I molecules that, through the action of bacterial BirA, have been biotinylated.

ASL disorder is associated with considerable clinical and genetic heterogeneity which is considered to reflect the extensive intragenic complementation occurring among different individual patients.

two protein subunits bind to form a dimer. Two dimers then bind to form the final tetramer.
The formation of the sorbitol dehydrogenase tetramer from its monomers via dimers.
A homotetrameric complex, beta-glucuronidase (a glycosidase ). Each subunit has the same amino acid sequence.
The heterotetrameric molecule haemoglobin , made up of four subunits of two different types (coloured red and blue .)