RESUMO
Conformation dynamics attributes to the biological functions of active proteins and conformation ensembles. The conformation ensembles include protein stable states (PSS) that can be measured by conventional structural biology approaches and the invisible protein states (IPS) that cannot be measured by conventional structural biology ones. The conformational exchange between IPS and PSS plays an important role in the biological functions of proteins. In this review, we briefly describe the basic properties of IPS and discuss its contribution to the development of the classical molecular recognition mechanism of “keylock hypothesis” and "induced fit hypothesis" into "conformational selection hypothesis". Furthermore, this review compares the advantages and disadvantages of the current structural biology approaches for investigating the conformational properties of IPS. Because of advanced NMR technology, the exploration of the conformational properties of IPS in experimental manner has become feasible. It is expected that the study of IPS and its function will not only help clarify the molecule recognition mechanism of proteins, but also provide a basis for guiding the design of targeted drugs.