2017
DOI: 10.1021/acs.jpclett.7b00127
|View full text |Cite
|
Sign up to set email alerts
|

Proton Dynamics in Protein Mass Spectrometry

Abstract: Native electrospray ionization/ion mobility-mass spectrometry (ESI/IM-MS) allows an accurate determination of low-resolution structural features of proteins. Yet, the presence of proton dynamics, observed already by us for DNA in the gas phase, and its impact on protein structural determinants, have not been investigated so far. Here, we address this issue by a multistep simulation strategy on a pharmacologically relevant peptide, the N-terminal residues of amyloid-β peptide (Aβ(1-16)). Our calculations reprod… Show more

Help me understand this report
View preprint versions

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

7
50
0

Year Published

2018
2018
2023
2023

Publication Types

Select...
5
1

Relationship

1
5

Authors

Journals

citations
Cited by 40 publications
(57 citation statements)
references
References 92 publications
7
50
0
Order By: Relevance
“…While the presence of the p6 domain had minimal effect on the oligomeric states observed, it did influence the charge state distribution. The multimodal charge state distribution observed for WT Gag is attributed to the presence of the intrinsically disordered p6 domain (37). As expected, dimerization depended on the well-characterized dimer interface in the C-terminal domain of CA, as WM-GagΔp6 was exclusively monomeric (Figures 2C1 and S3) (38,39).…”
Section: Resultssupporting
confidence: 65%
“…While the presence of the p6 domain had minimal effect on the oligomeric states observed, it did influence the charge state distribution. The multimodal charge state distribution observed for WT Gag is attributed to the presence of the intrinsically disordered p6 domain (37). As expected, dimerization depended on the well-characterized dimer interface in the C-terminal domain of CA, as WM-GagΔp6 was exclusively monomeric (Figures 2C1 and S3) (38,39).…”
Section: Resultssupporting
confidence: 65%
“…Native‐MS has been compared to fluorescence and CD spectroscopy in evaluating the effect of ammonium acetate on the conformation and the metal‐binding properties of two zinc‐finger domains, the nucleocapsid protein (NCp7, residues 12–55) of human immunodeficiency virus 1 and the specificity protein 1 (Sp1‐2, residues 565–595). The addition of increasing concentrations of ammonium acetate to protein‐Zn 2+ mixtures have a dramatic effect on the apparent affinity, as well as on the CSD, which is narrower and shifted toward lower charge states in the presence of the salt . Ammonium acetate is known to promote detection of non‐covalent complexes and native‐like protein conformations by native‐MS, thanks to counter‐ion binding at interfaces and to the possibility to modulate ionic strength without interfering with the ESI process .…”
Section: Comparison With Solution Methodsmentioning
confidence: 99%
“…Thus, the combined sets of results suggest that these specific protein–metal interactions are promoted by ammonium acetate in solution, by a mechanism mediated by conformational changes. The analysis has been extended to other salts of the Hofmeister series …”
Section: Comparison With Solution Methodsmentioning
confidence: 99%
See 2 more Smart Citations