Intrinsic Disorder and Protein Function

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How researchers see this paper

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Intrinsically unstructured proteins and their functions (2005, background): “jpg" NDATA ITEM> ]> The occurrence of unstructured regions of significant size (>50 residues) is surprisingly common in functional protein”
DFLpred: High-throughput prediction of disordered flexible linker regions in protein sequences (2016, neutral): “The newest release of DisProt database (Sickmeier et al., 2007), the main source of functionally annotated IDPs, lists >30 functions (Dunker et al., 2002) that have been assigned to about 1200 disordered regions.”
Mapping Residual Structure in Intrinsically Disordered Proteins at Residue Resolution Using Millisecond Hydrogen/Deuterium Exchange and Residue Averaging (2015, background): “Intrinsically disordered proteins contain regions that lack well-defined structure under in vivo or native in vitro conditions [1–3].”
PROFbval: predict flexible and rigid residues in proteins (2006, background): “The importance of flexibility is illustrated by many biological processes, including molecular recognition and catalytic activity (Demchenko, 2001; Dunker et al., 2002; Dyson andWright, 2005; Liu et al., 2002; Palmer, 2001; Tainer et al., 1984; Tompa, 2005), e.g. the flexibility of the switch II…”