Abstract

Transient complexes are crucial for diverse biological processes such as biochemical pathways and signaling cascades in the cell. Here, we give an overview of the transient interactions; the importance of transient inter-actions as drug targets; and the structural characteriz-ation of transient protein–protein complexes based on the geometrical and physicochemical features of the transient complexes ’ interfaces. To better understand and even-tually design transient protein–protein interactions (TPPIs), a molecular perspective of the protein–protein interfaces is necessary. Obtaining high-quality structures of protein–protein interactions could be one way of achieving this goal. After introducing the association kinetics of TPPIs, we elaborate on the experimental techniques detecting TPPIs in combination with the com-putational methods which classify transient and/or non-obligate complexes. In this review, currently available databases and servers that can be used to identify and predict TPPIs are also compiled.