Abstract (EN):
Protein–protein binding is one of the critical events in biology, and knowledge of proteic complexes
three-dimensional structures is of fundamental importance for the biochemical study of pharmacologic compounds.
In the past two decades there was an emergence of a large variety of algorithms designed to predict the structures of
protein–protein complexes—a procedure named docking. Computational methods, if accurate and reliable, could
play an important role, both to infer functional properties and to guide new experiments. Despite the outstanding
progress of the methodologies developed in this area, a few problems still prevent protein–protein docking to be a
widespread practice in the structural study of proteins. In this review we focus our attention on the principles that
govern docking, namely the algorithms used for searching and scoring, which are usually referred as the docking
problem. We also focus our attention on the use of a flexible description of the proteins under study and the use of
biological information as the localization of the hot spots, the important residues for protein–protein binding. The
most common docking softwares are described too.
Language:
English
Type (Professor's evaluation):
Scientific