Conformational changes in the side chains are essential for protein-protein binding. Rotameric states and unbound-to-bound conformational changes in the surface residues were systematically studied on a representative set of protein complexes. The side-chain conformations were mapped onto dihedral angles space. Rotamers were defined as the most probable conformation in a cluster. Probabilities of the rotamer transitions upon binding were calculated.


Tatsiana Kirys, Anatoly M. Ruvinsky, Alexander V. Tuzikov and Ilya A. Vakser
Rotamer libraries and probabilities of transition between rotamers for the side chains in protein–protein binding. Proteins 2012; 80:2089–2098.