A systematic analysis of intrinsic disorder in proteins
started at the turn of the century1–4 and still remains a
hot research topic.5 Only this year several papers covering
general aspects of protein disorder have been published5–
9 and the discussion on the fundamental
principles of disorder continues to unfold.10,11 PubMed
search with the keywords “intrinsically disordered protein
2012” and “intrinsically disordered protein 2013”
returned 525 and 305 entries, respectively (as of April
2013). The number of experimentally verified intrinsically
disordered proteins and regions is steadily increasing.
The DisProt database12 currently contains
annotations for 684 intrinsically disordered proteins,
1513 disordered regions, and describes 38 different biological
functions associated with disordered regions. The
more recently established IDEAL database also has a
number of useful annotations on disordered proteins.13
Such a high interest in this area of research triggered
rapid development of computational methods for prediction
of the location of disordered regions in proteins. The
recently published reviews and assessment papers14–18
altogether provide a comprehensive analysis of more than
fifty disorder prediction methods. An independent assessment
of the protein disorder methods within the scope of CASP started in 2002 and is now already in its sixth
round.18–22 This study analyzes the results obtained by
the 28 disorder prediction groups participating in CASP10