Neglected for a long time, highly flexible, intrinsically disordered proteins (IDPs), as well as flexible regions of complex protein machineries (IDRs), recently attracted the attention of the scientific community. Research in this field is blooming. Novel functional modules that are not yet described in the protein data bank (PDB) are beginning to be discovered. This is likely to be just a glimpse on the versatility through which function is encoded in the primary sequence of proteins not only through structure but also through disorder and flexibility. Many of the currently incurable diseases, such as cancer and neurodegenerative diseases, originate by misfuction of complex proteins lacking a stable three dimensional structure. The potential impact of shifting the focus to IDPs/IDRs as targets for drug discovery is extraordinary. To fully realize this objective a thorough understanding of their structural and dynamic properties is required.

Fascinated by this emerging field of research I like to contribute to it by development of improved NMR methods to exploit at best this highly powerful, sophisticated spectroscopic technique to look at intimate details of IDPs/IDRs.