Intrinsically disordered proteins: a 10-year recap.

By Peter Tompa. TIBS -Trends in Biochemical Sciences. Regular ed, 2012

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Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions (2017, background): “IDRs can be found in PDB as the regions that are missing in the X-ray crystal structures of proteins [25,20,26,27] or regions that are associated with high structural variability in the NMR models [28,29].”
Principles of protein structural ensemble determination. (2017, background): “The importance of using structural ensembles is particularly evident in the case of disordered proteins, which are a class of proteins that lack well-defined structures and instead populate a large number of conformationally heterogeneous states [7,8 ,9 ,10,11].”
Genome‐scale prediction of proteins with long intrinsically disordered regions (2014, background): “Some of the enriched functions that we found overlap with the results from the previous studies,3,33,75 including various DNA and RNA binding events that facilitate transcription, DNA repair, DNA replication, DNA recombination, and RNA metabolism; signal transduction via the GTPases and protein kina”
Intrinsically Disordered Proteins Studied by NMR Spectroscopy (2015, background): “335 Mihaly Varadi and Peter Tompa 12 Order and Disorder in the Replicative Complex of Paramyxoviruses .................................................................................. 351 Jenny Erales, David Blocquel, Johnny Habchi, Matilde Beltrandi, Antoine Gruet, Marion Dosnon, Christophe Bignon”