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.

Testa, L., Brocca, S., Santambrogio, C., D'Urzo, A., Habchi, J., Longhi, S., et al. (2013). Extracting structural information from charge-state distributions of intrinsically disordered proteins by non-denaturing electrospray-ionization mass spectrometry. INTRINSICALLY DISORDERED PROTEINS, 1(1) [10.4161/idp.25068].

Extracting structural information from charge-state distributions of intrinsically disordered proteins by non-denaturing electrospray-ionization mass spectrometry

BROCCA, STEFANIA;SANTAMBROGIO, CARLO;D'URZO, ANNALISA;GRANDORI, RITA
2013

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.
Articolo in rivista - Review Essay
native mass spectrometry, charge-state distributions, charge-to-mass relation, protein folding, solvent-accessible surface area, IDP compaction, intrinsically folded structural units, proteomics, Sic1, α-synuclein
English
Testa, L., Brocca, S., Santambrogio, C., D'Urzo, A., Habchi, J., Longhi, S., et al. (2013). Extracting structural information from charge-state distributions of intrinsically disordered proteins by non-denaturing electrospray-ionization mass spectrometry. INTRINSICALLY DISORDERED PROTEINS, 1(1) [10.4161/idp.25068].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/52036
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