Shapeshifting proteins: the role of structural disorder and conformational plasticity in physiology and disease

Intrinsically disordered proteins (IDPs) defy the conventional structure-function paradigm and do not autonomously fold up into unique 3D structures for carrying out functions. They exist as rapidly interconverting conformational ensembles and are thought to expand the functional repertoire of proteins. Such shapeshifting proteins are associated with a multitude of biological functions and a wide range of human diseases. The thematic issue on 'Shapeshifting Proteins' in Essays in Biochemistry includes some exciting and emerging aspects of this class of proteins. Articles in this issue provide current trends and contemporary views on various intriguing features of these proteins involving their unique structural and dynamical characteristics, misfolding and aggregation behavior, and their phase transitions into biomolecular condensates. I hope that this thematic issue will be of considerable interest to the practitioners in protein biochemistry and biophysics as well as to the researchers in other allied areas involving cell and molecular biology, neuroscience, virology, pathophysiology, and so forth.

Automated summary

Intrinsically disordered proteins (IDPs) are a class of proteins that expand the functional repertoire and are associated with various biological functions and human diseases. This thematic issue provides current trends and contemporary views on the unique structural and dynamical characteristics of these proteins, as well as their misfolding behavior, aggregation behavior, and phase transitions into biomolecular condensates.