Cooperative Conformational Changes in Globular Proteins

In globular proteins, the complicated steric arrangement of the polypeptide chain is determined by several interdependent cooperative interactions. These macromolecules are capable of reacting to changes in the environmental conditions such as temperature and pressure or the concentration of a wide range of compounds by changing their conformation and hence their biological and chemical properties. They are thus suitable for regulation processes or information storage in solution with a wide range of time constants. Environmental effects of this kind can be followed and explained in part at the molecular level by investigation of the time‐dependent reversible unfolding of a number of proteins that can be described to a good approximation by a strongly cooperative “all‐or‐none” transition between two states.