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Not all proteins form well defined three-dimensional structures in their native states. Some amino-acid sequences appear to strongly favour the disordered state, whereas some can apparently transition between disordered and ordered states under the influence of changes in the biological environment, thereby playing an important role in processes such as signalling. Although important biologically, for the structural biologist disordered regions of proteins can be disastrous even preventing successful structure determination. The accurate prediction of disorder is therefore important, not least for directing the design of expression constructs so as to maximize the chances of successful structure determination. Such design criteria have become integral to the construct-design strategies of laboratories within the Structural Proteomics In Europe (SPINE) consortium. This paper assesses the current state of the art in disorder prediction in terms of prediction reliability and considers how best to use these methods to guide construct design. Finally, it presents a brief discussion as to how methods of prediction might be improved in the future.

Original publication




Journal article


Acta crystallographica. Section D, Biological crystallography

Publication Date





1260 - 1266


Division of Structural Biology, University of Oxford, Wellcome Trust Centre for Human Genetics, Oxford, England.


Proteins, Recombinant Proteins, Data Collection, Reproducibility of Results, Computational Biology, Protein Conformation, Protein Folding, Algorithms, Forecasting, Models, Structural, Computer Simulation