Native mass spectrometry (MS) has become a central tool of structural proteomics, but its applicability to the peculiar class of intrinsically disordered proteins (IDPs) is still object of debate. IDPs lack an ordered tridimensional structure and are characterized by high conformational plasticity. Since they represent valuable targets for cancer and neurodegeneration research, there is an urgent need of methodological advances for description of the conformational ensembles populated by these proteins in solution. However, structural rearrangements during electrospray-ionization (ESI) or after the transfer to the gas phase could affect data obtained by native ESI-MS. In particular, charge-state distributions (CSDs) are affected by protein conformation inside ESI droplets, while ion mobility (IM) reflects protein conformation in the gas phase. This review focuses on the available evidence relating IDP solution ensembles with CSDs, trying to summarize cases of apparent consistency or discrepancy. The protein-specificity of ionization patterns and their responses to ligands and buffer conditions suggests that CSDs are imprinted to protein structural features also in the case of IDPs. Nevertheless, it seems that these proteins are more easily affected by electrospray conditions, leading in some cases to rearrangements of the conformational ensembles. [Figure not available: see fulltext.]

Natalello, A., Santambrogio, C., Grandori, R. (2017). Are Charge-State Distributions a Reliable Tool Describing Molecular Ensembles of Intrinsically Disordered Proteins by Native MS?. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 28(1), 21-28 [10.1007/s13361-016-1490-1].

Are Charge-State Distributions a Reliable Tool Describing Molecular Ensembles of Intrinsically Disordered Proteins by Native MS?

NATALELLO, ANTONINO
Primo
;
SANTAMBROGIO, CARLO
Secondo
;
GRANDORI, RITA
Ultimo
2017

Abstract

Native mass spectrometry (MS) has become a central tool of structural proteomics, but its applicability to the peculiar class of intrinsically disordered proteins (IDPs) is still object of debate. IDPs lack an ordered tridimensional structure and are characterized by high conformational plasticity. Since they represent valuable targets for cancer and neurodegeneration research, there is an urgent need of methodological advances for description of the conformational ensembles populated by these proteins in solution. However, structural rearrangements during electrospray-ionization (ESI) or after the transfer to the gas phase could affect data obtained by native ESI-MS. In particular, charge-state distributions (CSDs) are affected by protein conformation inside ESI droplets, while ion mobility (IM) reflects protein conformation in the gas phase. This review focuses on the available evidence relating IDP solution ensembles with CSDs, trying to summarize cases of apparent consistency or discrepancy. The protein-specificity of ionization patterns and their responses to ligands and buffer conditions suggests that CSDs are imprinted to protein structural features also in the case of IDPs. Nevertheless, it seems that these proteins are more easily affected by electrospray conditions, leading in some cases to rearrangements of the conformational ensembles. [Figure not available: see fulltext.]
Articolo in rivista - Review Essay
Conformational effects; ESI mechanism; Intermediate regime; Protein structure; Structural disorder;
Conformational effects; ESI mechanism; Intermediate regime; Protein structure; Structural disorder; Structural Biology; Spectroscopy
English
2017
28
1
21
28
reserved
Natalello, A., Santambrogio, C., Grandori, R. (2017). Are Charge-State Distributions a Reliable Tool Describing Molecular Ensembles of Intrinsically Disordered Proteins by Native MS?. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 28(1), 21-28 [10.1007/s13361-016-1490-1].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/150727
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