Probing the Stability of Insulin Oligomers Using Electrospray Ionization Ion Mobility Mass Spectrometry

2015 ◽  
Vol 21 (6) ◽  
pp. 759-774 ◽  
Author(s):  
Uday Kumar Boga Raja ◽  
Srilakshmi Injeti ◽  
Tiffany Culver ◽  
Jacob W. McCabe ◽  
Laurence A. Angel
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Ionization ◽  
Ion Mobility ◽  
Ion Mobility Mass Spectrometry ◽  
The Stability

Ligand induced structural isomerism in phosphine coordinated gold clusters revealed by ion mobility mass spectrometry

2017 ◽  
Vol 53 (53) ◽  
pp. 7389-7392 ◽  
Author(s):  
Marshall R. Ligare ◽  
Erin S. Baker ◽  
Julia Laskin ◽  
Grant E. Johnson
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Ionization ◽  
Ion Mobility Spectrometry ◽  
Ion Mobility ◽  
Gold Clusters ◽  
Ion Mobility Mass Spectrometry ◽  
Structural Isomerism

Structural isomerism in ligated gold clusters is revealed using electrospray ionization ion mobility spectrometry mass spectrometry.

Characterization of superoxide dismutase 1 (SOD-1) by electrospray ionization-ion mobility mass spectrometry

2013 ◽  
Vol 48 (1) ◽  
pp. 60-67 ◽  
Author(s):  
Marta Borges-Alvarez ◽  
Fernando Benavente ◽  
Marta Vilaseca ◽  
José Barbosa ◽  
Victoria Sanz-Nebot
Keyword(s):  
Mass Spectrometry ◽  
Superoxide Dismutase ◽  
Electrospray Ionization ◽  
Ion Mobility ◽  
Ion Mobility Mass Spectrometry ◽  
Superoxide Dismutase 1

Shapes of supramolecular cages by ion mobility mass spectrometry

2012 ◽  
Vol 48 (37) ◽  
pp. 4423-4425 ◽  
Author(s):  
Jakub Ujma ◽  
Martin De Cecco ◽  
Oleg Chepelin ◽  
Hannah Levene ◽  
Chris Moffat ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Supramolecular Complexes ◽  
Ion Mobility Mass Spectrometry ◽  
Structural Differences ◽  
Self Assembled ◽  
The Stability

Ion mobility mass spectrometry distinguishes between isobaric supramolecular complexes, revealing subtle structural differences and their effect on the stability of self assembled architectures.

scholarly journals Correlating glycoforms of DC-SIGN with stability using a combination of enzymatic digestion and ion mobility MS

2020 ◽  
Author(s):  
Hsin-Yung Yen ◽  
Idlir Liko ◽  
Joseph Gault ◽  
Di Wu ◽  
Weston B. Struwe ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Gas Phase ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Enzymatic Digestion ◽  
Ion Mobility Mass Spectrometry ◽  
Structural Detail ◽  
The Core ◽  
Glycosylation Sites ◽  
The Stability

AbstractThe immune scavenger protein DC-SIGN interacts with glycosylated proteins and has a putative role in facilitating viral infection. How these recognition events take place with different viruses is not clear and the effects of glycosylation on the folding and stability of DC-SIGN have not been reported. Here, we develop and apply a mass spectrometry-based approach to both uncover and characterise the effects of O-glycans on the stability of DC-SIGN. We first quantify the Core 1 & 2 O-glycan structures on the carbohydrate recognition and extracellular domains of the protein via sequential exoglycosidase sequencing. We then use ion mobility mass spectrometry to show how specific O-glycans, and/or single monosaccharide substitutions, alter both the overall collision cross section and the gas-phase stability of the glycoprotein isoforms of DC-SIGN. We find that rather than the mass or length of glycoprotein modifications, the stability of DC-SIGN is better correlated with the number of glycosylation sites. Collectively, our results exemplify a combined multi-dimensional MS approach, proficient in evaluating protein stability in response to both glycoprotein macro- and micro-heterogeneity and adding structural detail to the infection enhancer DC-SIGN.

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