Cooperative conformational transitions of linear biopolymers.

Abstract

AbstractConformational transitions in proteins, nucleic acids, and other biopolymers evidently play a decisive role in many biological processes, particularly in control processes. They often proceed cooperatively, i.e. the elementary process of the transition of an individual segment of these macromolecules in influenced by the state of other segments via intramolecular interactions. In general, the segments favor the same state as their neighbours. The resulting equilibrium properties of cooperative systems, e.g. the sharpness of the transitions and their dependence on the chain length, can be quantitatively explained for linear systems by the linear Ising model. The molecular causes of the cooperativity can be explained for simple model polymers.