It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

Research of a past decade and a half leaves no doubt that complete understanding of
protein functionality requires close consideration of the fact that many functional proteins do …

Proteins, with their seemingly limitless functional diversity, are major players in the
maintenance of life. The ability of proteins to fulfill these various biological functions is …

Intrinsically disordered proteins (IDPs) do not have rigid 3D structures, showing changes in
their folding depending on the environment or ligands. Intrinsically disordered proteins are …

Structural disorder of functional proteins under physiological conditions is widespread within
eukaryotic proteomes. The lack of stable tertiary and secondary structure offers a variety of …

In addition to the “traditional” proteins characterized by the unique crystal-like structures
needed for unique functions, it is increasingly recognized that many proteins or protein …

Intrinsically disordered proteins (IDPs) or natively unfolded proteins do not undergo
autonomous folding into a well-defined 3-D structure and challenge the conventional …

For more than a century, molecular and structural biology, biochemistry, and protein
biophysics have been dominated by a “rigid” or “semi-rigid” view of a functional protein …

Many full-length proteins and protein regions lack stable tertiary and/or secondary structure
under physiological conditions in vitro. These proteins and regions, known as intrinsically …

The existence and functioning of intrinsically disordered proteins (IDPs) challenge the
classical structure-function paradigm that equates function with a well-defined 3D structure …