title: Proteomic methods for the identification of intrinsically disordered proteins.
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.
authors: Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary.
authors: Agnes
authors: A
authors: Tantos
authors: Peter
authors: P
authors: Tompa
mesh_terms: D000818:Animals; D001419:Bacteria / Q000166:cytology / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D007525:Isoelectric Focusing; D051379:Mice; D041681:NIH 3T3 Cells; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D015003:Yeasts / Q000166:cytology / Q000235:genetics
chemical_list: D011506:Proteins