Many proteins and protein segments cannot attain a single stable three-dimensional
structure under physiological conditions; instead, they adopt multiple interconverting …

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 …

Intrinsically disordered proteins, defying the traditional protein structure–function paradigm,
are a challenge to study experimentally. Because a large part of our knowledge rests on …

Interactions between proteins are orchestrated in a precise and time-dependent manner,
underlying cellular function. The binding affinity, defined as the strength of these …

Protein intrinsic disorder is becoming increasingly recognized in proteomics research. While
lacking structure, many regions of disorder have been associated with biological function …

This review describes the family of intrinsically disordered proteins, members of which fail to
form rigid 3-D structures under physiological conditions, either along their entire lengths or …

The abundant existence of proteins and regions that possess specific functions without
being uniquely folded into unique 3D structures has become accepted by a significant …

Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structures under
physiological conditions in vitro. They are highly abundant in nature and their functional …

The transcription factor, p53, is critical for many important cellular functions involved in
genome integrity, including cell cycle control, DNA damage response, and apoptosis …

The ideas that proteins might possess specific functions without being uniquely folded into
rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of …