Document Type
Article
Publication Date
2013
Keywords
IDP Compaction, Sic1, Charge-state Distributions, Charge-to-mass Relation, Intrinsically Folded Structural Units, Native Mass Spectrometry, Protein Folding, Proteomics, Solvent-accessible Surface Area, α-Synuclein
Digital Object Identifier (DOI)
https://doi.org/10.4161%2Fidp.25068
Abstract
Intrinsically disordered proteins (IDPs) exert key biological functions but tend to escape identification and characterization due to their high structural dynamics and heterogeneity. The possibility to dissect conformational ensembles by electrospray-ionization mass spectrometry (ESI-MS) offers an attracting possibility to develop a signature for this class of proteins based on their peculiar ionization behavior. This review summarizes available data on charge-state distributions (CSDs) obtained for IDPs by non-denaturing ESI-MS, with reference to globular or chemically denatured proteins. The results illustrate the contributions that direct ESI-MS analysis can give to the identification of new putative IDPs and to their conformational investigation.
Rights Information
This work is licensed under a Creative Commons Attribution-Noncommercial 3.0 License
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Intrinsically Disordered Proteins, v. 1, issue 1, art. e25068
Scholar Commons Citation
Testa, Lorenzo; Brocca, Stefania; Santambrogio, Carlo; D'Urzo, Annalisa; Habchi, Johnny; Longhi, Sonia; Uversky, Vladimir N.; and Grandori, Rita, "Extracting Structural Information from Charge-state Distributions of Intrinsically Disordered Proteins by Non-denaturing Electrospray-ionization Mass Spectrometry" (2013). Molecular Medicine Faculty Publications. 452.
https://digitalcommons.usf.edu/mme_facpub/452
