In the last years there has been an increasing amount of experimental
evidence pointing out that a large number of proteins are either fully or partially
disordered. Intrinsically disordered proteins are ubiquitous proteins that fulfil biological
functions while lacking highly populated and uniform secondary and tertiary structure
under physiological conditions. Despite the frequent occurrence of structural disorder,
disordered regions are still poorly detected. Recognition of disordered regions in a
protein is instrumental for reducing spurious sequence similarity during sequence
comparisons between disordered regions and ordered ones, and for delineating
boundaries of protein domains amenable to crystallization. As none of available
methods for prediction of protein disorder can be taken as fully reliable on its own, we
present a brief overview of current methods and highlight their subjacent philosophy.
We show a few practical examples of how they can be combined to avoid respective
pitfalls and achieve more reliable predictions. We also describe currently available
methods for the identification of regions involved in induced folding and provide a few
practical examples in which the accuracy of predictions was experimentally confirmed.
Intrinsic disorder, intrinsically disordered proteins, intrinsically
disordered regions, disorder prediction, structure prediction, metaservers,
Molecular Recognition Elements, MoREs, Molecular Recognition Features
(MoRFs), prediction of MoREs/MoRFs, induced folding, coupled binding and
folding, prediction of induced folding regions.
Architecture et Fonction des Macromolécules Biologiques, UMR 7257 CNRS and Aix-Marseille Université, 163 Avenue de Luminy, Case 932, 13288 Marseille Cedex 09, France.