Stable interactions involve proteins that interact for a long time, taking part of permanent complexes as subunits, in order to carry out structural or functional roles.
Another important distinction to identify protein-protein interactions is the way they have been determined, since there are techniques that measure direct physical interactions between protein pairs, named “binary” methods, while there are other techniques that measure physical interactions among groups of proteins, without pairwise determination of protein partners, named “co-complex” methods. In addition to the conventional complexes, as enzyme-inhibitor and antibody-antigen, interactions can also be established between domain-domain and domain-peptide. A protein complex assembly can result in the formation of homo-oligomeric or hetero-oligomeric complexes. To describe the types of protein–protein interactions (PPIs) it is important to consider that proteins can interact in a 'transient' way (to produce some specific effect in a short time) or to interact with other proteins in a 'stable' way to build multiprotein complexes that are molecular machines within the living systems.
0 kommentar(er)
