Tag Archives: Intrinsically Disordered Proteins

The Emerging Disorder-Function Paradigm

It’s rare to find a paper that connects all of the diverse areas of research of OPIG, but “The rules of disorder or why disorder rules” by Gsponer and Babu (2009) is one such paper. Protein folding, protein-protein interaction networks, protein loops (Schlessinger et al., 2007), and drug discovery all play a part in this story. What’s great about this paper is that it gives numerous examples of proteins and the evidence supporting that they are partially or completely unstructured. These are the so-called intrinsically unstructured proteins or IUPs, although more recently they are also being referred to as intrinsically disordered proteins, or IDPs. Intrinsically disordered regions (IDRs) “are polypeptide segments that do not contain sufficient hydrophobic amino acids to mediate co-operative folding” (Babu, 2016).

Such proteins contradict the classic “lock and key” hypothesis of Fischer, and challenge Continue reading