Proteomic methods for the identification of intrinsically disordered proteins.

TitleProteomic methods for the identification of intrinsically disordered proteins.
Publication TypeJournal Article
Year of Publication2012
AuthorsTantos, Á., and P. Tompa
JournalMethods Mol Biol
Volume896
Pagination429-37
Date Published2012
Type of Articleidp
ISSN1940-6029
KeywordsAnimals, Bacteria, Electrophoresis, Polyacrylamide Gel, Hot Temperature, Isoelectric Focusing, Mice, NIH 3T3 Cells, Proteins, Proteomics, Yeasts
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.

DOI10.1007/978-1-4614-3704-8_29
Alternate JournalMethods Mol. Biol.
PubMed ID22821542