Journal ArticleDOI
Probing conformational changes in proteins by mass spectrometry
TLDR
The authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.Abstract:
Mass spectrometry has found wide application for the elucidation of the primary structures of proteins. However, with the exception of topographical studies of membrane-bound proteins, mass spectrometry has not previously been utilized to obtain information concerning in three-dimensional conformation of proteins. In the present communication, the authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.read more
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Journal ArticleDOI
26 kDa endochitinase from barley seeds: Real-time monitoring of the enzymatic reaction and substrate binding experiments using electrospray ionization mass spectrometry
TL;DR: This study is the first enzymatic characterization of chitinase exclusively by electrospray ionization mass spectrometry (ESI-MS), and the binding free energy values obtained for E67Q were found to be comparable to those previously obtained in liquid phase, but less dependent upon the chain length of the oligosaccharides.
Journal ArticleDOI
Following Structural Changes by Thermal Denaturation Using Trapped Ion Mobility Spectrometry-Mass Spectrometry.
TL;DR: In a single experiment, this technology provides a detailed view of the solution, protein structural landscape (mobility vs solution temperature vs relative intensity for each charge state) and at least six structural transitions of BSA.
Journal ArticleDOI
Critical examination of gas-phase protein conformation/multimer ion formation by electrospray ion mobility-mass spectrometry.
Kent J. Gillig,Chung-Hsuan Chen +1 more
TL;DR: The focus of this work will be to correctly distinguish truly different ion conformations formed by ESI versus homomultimeric complexes with the same m/z, and suggest that the total IM-MS distribution for a protein is the complex result of individual MCMs either surviving until detection or dissociating into lower order multimers or a number of product ions for each m/Z.
Journal ArticleDOI
The Effects of Trivalent Lanthanide Cationization on the Electron Transfer Dissociation of Acidic Fibrinopeptide B and its Analogs.
TL;DR: Adduction with trivalent lanthanide metal ions is a promising tool for sequence analysis of acidic peptides by ETD and with the exception of the results for Eu(III), metallated peptide ion formation by ESI, ETD fragmentation efficiencies, and product ion formation are unaffected by the identity of the Lanthanide cation.
Journal ArticleDOI
Hydrogen/Deuterium and 16O/18O-Exchange Mass Spectrometry Boosting the Reliability of Compound Identification.
Yury Kostyukevich,Alexander Zherebker,Alexey A. Orlov,Oxana Kovaleva,Tatyana I. Burykina,Boris Isotov,Evgeny N. Nikolaev +6 more
TL;DR: An approach utilizing the selection of structural candidates from database based on the number of functional groups and analysis of isotope labels distribution among fragments allows reducing of the search space by the factor of 10 and considerably increases the reliability of the compound identification.
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