A major challenge in the post-genome era will be determination of the functions of the
encoded protein sequences. Since it is generally assumed that the function of a protein is …

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

Intrinsically disordered proteins and protein regions (IDPs/IDRs) exist without a single well-
defined conformation. They carry out important biological functions with multifaceted roles …

The coronavirus nucleocapsid (N) is a structural protein that forms complexes with genomic
RNA, interacts with the viral membrane protein during virion assembly and plays a critical …

Proteins can exist in a trinity of structures: the ordered state, the molten globule, and the
random coil. The five following examples suggest that native protein structure can …

Abstract “Natively unfolded” proteins occupy a unique niche within the protein kingdom in
that they lack ordered structure under conditions of neutral pH in vitro. Analysis of amino …

Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …

Intrinsic disorder refers to segments or to whole proteins that fail to self‐fold into fixed 3D
structure, with such disorder sometimes existing in the native state. Here we report data on …

The experimental material accumulated in the literature on the conformational behavior of
intrinsically unstructured (natively unfolded) proteins was analyzed. Results of this analysis …

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 …