The induced fit theory explains the formation of a protein-ligand complex (e.g. an enzyme-substrate complex in enzyme-catalyzed reactions).
It was postulated by Daniel E. Koshland in 1958 and is an extension of the lock and key principle : protein (e.g. an enzyme ) and a ligand (or substrate ) are no longer viewed as static. Both interact when they approach each other and thus change their conformations accordingly, which is the first time that the protein-ligand complex can form.
However, this induced adaptation does not apply to all ligand-receptor complexes. The change in conformation of both partners is often subject to natural limits and so it is often at the expense of specificity and affinity .
- ^ DE Koshland: Application of a Theory of Enzyme Specificity to Protein Synthesis. In: Proc Natl Acad Sci USA . tape 44 , 1958, pp. 98-104 , doi : 10.1073 / pnas.44.2.98 .