We recently had the wonderful opportunity to speak with Peter Wright about the history and future of the IDP field. Wright is a Professor in the Department of Integrative Structural and Computational Biology at the Scripps Research Institute in La Jolla; he published seminal works in the IDP literature and has been instrumental in the evolution of the field. An excerpt from the interview is provided here. To read the full article, go to the Subgroup page.
Q. Can you describe the initial reception to the idea of IDPs having function in their disordered state?
Complete and utter skepticism! There was the thought that IDPs wouldn’t survive in the cell... The dogma that prevailed was that structure equals function, and that recognition was by lock and key. Those ideas were firmly ingrained in the community, and they didn’t see that disorder had any role in biology.
What changed that view is the huge number of examples of IDPS that have been identified and studied in detail. There’s been an explosion of data over the last few years on proteins that are clearly disordered and have extremely important biological functions.
Q: Where do you think IDP research will go in the future?
One important thing is development of technologies to characterize full-length proteins. Huge numbers of eukaryotic proteins have both globular domains and disordered regions. How do we characterize these, beyond reduction domain by domain, region by region, to understand how the whole protein works synergistically? The other one is going to be tough: addressing structural and biophysical questions on IDPs in their native environment in the cell. Are interaction domains of IDPs always bound to partners and folded? To what extent are they free and flexible? The challenge of studying regulatory and signaling IDPs in their native environment will be their low concentrations—developing technology for such studies will be critical.
—Lauren Ann Metskas, Graduate Student Representative