Literature DB >> 11791572

Monitoring structural changes of proteins in an ion trap over approximately 10-200 ms: unfolding transitions in cytochrome c ions.

E R Badman1, C S Hoaglund-Hyzer, D E Clemmer.   

Abstract

A new technique for studying the time dependence of conformational changes of gas-phase protein ions is described. In this approach, a short pulse of electrosprayed protein ions is introduced into an ion trap and stored. After a defined time period, the distribution of ions is ejected from the trap into an ion mobility/time-of-flight mass spectrometer. Combined measurements of mobilities and flight times in the mass spectrometer provide information about the abundances of different conformer types and charge-state distributions. By varying the storage time in the trap, it is possible to monitor changes in ion conformation that occur over extended time periods (approximately 10-200 ms). The method is demonstrated by examining changes in cytochrome c ion conformations for the +7 to +10 charge states.

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Year:  2001        PMID: 11791572     DOI: 10.1021/ac010744a

Source DB:  PubMed          Journal:  Anal Chem        ISSN: 0003-2700            Impact factor:   6.986


  48 in total

1.  The role of acidic residues and of sodium ion adduction on the gas-phase H/D exchange of peptides and peptide dimers.

Authors:  John C Jurchen; Russell E Cooper; Evan R Williams
Journal:  J Am Soc Mass Spectrom       Date:  2003-12       Impact factor: 3.109

2.  Ion mobility-mass spectrometry reveals conformational changes in charge reduced multiprotein complexes.

Authors:  Russell E Bornschein; Suk-Joon Hyung; Brandon T Ruotolo
Journal:  J Am Soc Mass Spectrom       Date:  2011-07-16       Impact factor: 3.109

Review 3.  Biomolecule analysis by ion mobility spectrometry.

Authors:  Brian C Bohrer; Samuel I Merenbloom; Stormy L Koeniger; Amy E Hilderbrand; David E Clemmer
Journal:  Annu Rev Anal Chem (Palo Alto Calif)       Date:  2008       Impact factor: 10.745

4.  Effects of ion/ion proton transfer reactions on conformation of gas-phase cytochrome c ions.

Authors:  Qin Zhao; Gregg M Schieffer; Matthew W Soyk; Timothy J Anderson; R S Houk; Ethan R Badman
Journal:  J Am Soc Mass Spectrom       Date:  2010-03-31       Impact factor: 3.109

5.  Effects of select anions from the Hofmeister series on the gas-phase conformations of protein ions measured with traveling-wave ion mobility spectrometry/mass spectrometry.

Authors:  Samuel I Merenbloom; Tawnya G Flick; Michael P Daly; Evan R Williams
Journal:  J Am Soc Mass Spectrom       Date:  2011-09-13       Impact factor: 3.109

6.  Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues.

Authors:  Yu Sun; Siavash Vahidi; Modupeola A Sowole; Lars Konermann
Journal:  J Am Soc Mass Spectrom       Date:  2015-09-14       Impact factor: 3.109

7.  Evaluation of ion mobility spectroscopy for determining charge-solvated versus salt-bridge structures of protonated trimers.

Authors:  Richard L Wong; Evan R Williams; Anne E Counterman; David E Clemmer
Journal:  J Am Soc Mass Spectrom       Date:  2005-07       Impact factor: 3.109

8.  Multidimensional separations of ubiquitin conformers in the gas phase: relating ion cross sections to H/D exchange measurements.

Authors:  Errol W Robinson; Evan R Williams
Journal:  J Am Soc Mass Spectrom       Date:  2005-09       Impact factor: 3.109

9.  Assessing the peak capacity of IMS-IMS separations of tryptic peptide ions in He at 300 K.

Authors:  Samuel I Merenbloom; Brian C Bohrer; Stormy L Koeniger; David E Clemmer
Journal:  Anal Chem       Date:  2007-01-15       Impact factor: 6.986

10.  Noncovalent protein tetramers and pentamers with "n" charges yield monomers with n/4 and n/5 charges.

Authors:  Richard L Beardsley; Christopher M Jones; Asiri S Galhena; Vicki H Wysocki
Journal:  Anal Chem       Date:  2009-02-15       Impact factor: 6.986

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