scholarly journals Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry

2007 ◽  
Vol 18 (12) ◽  
pp. 2180-2190 ◽  
Author(s):  
David P. Smith ◽  
Kevin Giles ◽  
Robert H. Bateman ◽  
Sheena E. Radford ◽  
Alison E. Ashcroft
Keyword(s):  
Mass Spectrometry ◽  
Protein Folding ◽  
Electrospray Ionization ◽  
Ion Mobility Spectrometry ◽  
Ion Mobility ◽  
Conformational States

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.

scholarly journals Analysis of Protein Folding Equilibria by Nano-Electrospray-Ionization Mass Spectrometry

2002 ◽  
Vol 16 (3-4) ◽  
pp. 361-370 ◽  
Author(s):  
Irena Matecko ◽  
Norbert Müller ◽  
Rita Grandori
Keyword(s):  
Mass Spectrometry ◽  
Protein Folding ◽  
Electrospray Ionization ◽  
Electrospray Ionization Mass Spectrometry ◽  
Tertiary Structure ◽  
Molten Globule ◽  
Ionization Mass Spectrometry ◽  
Ionization Mass ◽  
Conformational States ◽  
Esi Ms

This paper summarizes recent findings from our group concerning applications of electrospray-ionization mass spectrometry (ESI-MS) to the study of protein folding. Nano-ESI-MS was employed for the investigation of protein conformational states under varying solvent conditions and at varying values of the instrumental parameters. The effect of trifluoroethanol (TFE) on a peptide and acid-unfolded cytochromec(cytc), monitored by circular dichroism (CD) and time-of-flight ESI-MS, illustrates the specificity of the latter technique for features of protein tertiary structure. Measurements on marginally stable protein states indicate that it is possible to identify operational conditions for nano-ESI-MS in which none of the instrumental parameters limits conformational stability in the protein sample. Results described here show that changes in the charge-state distributions (CSDs) under controlled conditions allow not only discriminating between native and denatured states, but also monitoring minor conformational changes, like the transition from molten globule to native state. These studies underscore the potential of mass spectrometry methods for the analysis of heterogeneous samples and, in particular, for the characterization of dynamic equilibria involving different conformational states.

Electrospray ionization-ion mobility spectrometry–high resolution tandem mass spectrometry with collision-induced charge stripping for the analysis of highly multiply charged intact polymers

The Analyst ◽  
2019 ◽  
Vol 144 (10) ◽  
pp. 3428-3435 ◽  
Author(s):  
Yuka Ozeki ◽  
Mizuki Omae ◽  
Shinya Kitagawa ◽  
Hajime Ohtani
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
Tandem Mass Spectrometry ◽  
Electrospray Ionization ◽  
Ion Mobility Spectrometry ◽  
Ion Mobility ◽  
Tandem Mass ◽  
Multiply Charged ◽  
Charged Polymers ◽  
Induced Charge

Analysis of highly multiply charged polymers by IMS-MS/MS with collision-induced charge stripping.

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