Introduction: Intrinsically disordered proteins (IDPs) and intrinsically disordered protein
regions (IDPRs) have gained wide recognition over the past decade due to their versatile …

It is now widely recognized that intrinsically unstructured (or disordered) proteins (IUPs or
IDPs) are found in organisms from all kingdoms of life. In eukaryotes, IUPs are highly …

At the turn of this century, cardinal changes took place in the perceptions of the structure and
function of proteins, as well as in the organizational principles of membrane-less organelles …

Proteins are heteropolymers that play important roles in virtually every biological reaction.
While many proteins have well-defined three-dimensional structures that are inextricably …

Instrumental techniques for analyzing intrinsically disordered proteins The recently
recognized phenomenon of protein intrinsic disorder is gaining significant interest among …

Abstract Background Intrinsically disordered proteins (IDPs) and intrinsically disordered
regions (IDRs) lack stable tertiary and/or secondary structure yet fulfills key biological …

Much of our current knowledge of biological chemistry is founded in the structure-function
relationship, whereby sequence determines structure that determines function. Thus, the …

A growing number of proteins are being identified that are biologically active though
intrinsically disordered, in sharp contrast with the classic notion that proteins require a well …

Recognition of the natural abundance and functional importance of intrinsically disordered
proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions …

Intrinsic disorder is a natural feature of polypeptide chains, resulting in the lack of a defined
three-dimensional structure. Conformational changes in intrinsically disordered regions of a …