Tetramers are molecules that consist of four structural subunits or monomers bound together. These subunits can be of any type and can be identical or heterogeneous. The term "tetramer" specifically refers to the quaternary structure of a molecule and is often used in the context of proteins, where the monomers are protein subunits.
In proteins, tetramers can form through various non-covalent interactions, such as hydrogen bonds, hydrophobic interactions, and Van der Waals forces. These interactions stabilize the association of the four subunits, allowing them to function as a single unit with unique properties and functions. Tetramers can be involved in various biological processes, including enzyme activity, regulation, and signaling.
Examples of well-known tetramers include hemoglobin, which consists of two alpha and two beta subunits, and DNA polymerase, which contains four subunits. Tetramers can also be formed by other types of molecules, such as nucleic acids, in which four nucleotide units are bound together.
Studying the structure and function of tetramers is of great importance in various fields, including biochemistry, structural biology, and drug discovery. Understanding the formation and interactions of tetramers provides insights into their physiological roles and potential therapeutic targets.
