Abstract
Intrinsically disordered proteins (IDPs) lack fixed 3D structure under physiological conditions, yet they often carry out critically important physiological functions. The first few disordered proteins have been discovered one-by-one from clues that suggested that a protein lacks structure. Since bioinformatic predictions suggest that a large portion of eukaryotic proteomes contains significant levels of protein disorder, a reliable method for the large-scale separation and identification of these proteins is needed. IDPs do not undergo large-scale structural changes and aggregation at low pH or elevated temperatures. Thus, such proteins are likely to remain soluble under these extreme conditions, making acid treatment and/or heat treatment suitable for substantial enrichment of intrinsically unfolded proteins in the soluble fraction.
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Tantos, A., Tompa, P. (2012). Proteomic Methods for the Identification of Intrinsically Disordered Proteins. In: Uversky, V., Dunker, A. (eds) Intrinsically Disordered Protein Analysis. Methods in Molecular Biology, vol 896. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-3704-8_29
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DOI: https://doi.org/10.1007/978-1-4614-3704-8_29
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