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

Intrinsically Disordered Proteins
Lorenzo TestaRita Grandori

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.

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Citations

Apr 2, 2019·The FEBS Journal·Frank Gondelaud, Sylvie Ricard-Blum
May 1, 2020·The Journal of Biological Chemistry·Nicklas ÖsterlundCecilia Emanuelsson
Nov 2, 2016·Journal of Biochemistry·Tomoji SuenagaKazutaka Murayama
Apr 14, 2017·The Journal of Cell Biology·Katerina E ChatziAnastassios Economou
Oct 23, 2019·International Journal of Molecular Sciences·Roberta CortiValeria Cassina
Apr 13, 2021·Frontiers in Molecular Biosciences·Chandan ThapaUlla Pentikäinen
Dec 17, 2014·Journal of the American Society for Mass Spectrometry·Annalisa D'UrzoRita Grandori
Sep 3, 2021·Chemical Reviews·Amber D Rolland, James S Prell
Oct 5, 2021·Acta Crystallographica. Section F, Structural Biology Communications·Pieter De BruynRemy Loris

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Methods Mentioned

BETA
X-ray
circular
nuclear magnetic resonance
size-exclusion
NMR

Software Mentioned

SASA

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