Recognition between disordered polypeptide chains from cleavage of an alpha/beta domain: self-versus non-self-association.

Advances in structural biology have provoked a re-evaluation of the biological significance of the disordered state of proteins. We believe that the rules that govern structure, stability and kinetics in the molecular recognition between disordered polypeptide chains can be elucidated by studying processes that couple association with folding. The reassembly of single domain proteins by fragment complementation provides an excellent opportunity to study them.