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
Citations
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Journal ArticleDOI
An extended mass range quadrupole for electrospray mass spectrometry
B. A. Collings,Donald J. Douglas +1 more
TL;DR: In this paper, the mass range of a quadrupole mass spectrometer with an eleetrospray source was increased from m/z 4000 tom/z 8585 by lowering the radio frequency of the quadrupoles power supply from 1.00 MHz to 683 kHz.
Journal ArticleDOI
Charging of Proteins in Native Mass Spectrometry
Anna C. Susa,Zijie Xia,Henry Y. H. Tang,Henry Y. H. Tang,John A. Tainer,John A. Tainer,Evan R. Williams +6 more
TL;DR: Results provide compelling evidence that proton transfer between ammonia and protein ions does not limit protein ion charge in native electrospray ionization and indicate that droplet charge limits protein ion charges in native mass spectrometry.
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Metal exchange in metallothioneins – a novel structurally significant Cd5 species in the alpha domain of human metallothionein 1a
TL;DR: Evidence from indirect 1H‐113Cd HSQC NMR spectra suggests that the coordination environment of the additional Cd2+ is not tetrahedral to four thiolates, as is the case with the four Cd 2+ ions in the Cd4α‐MT, but has two thiolate ligands as part of its ligand environment, with additional coordination to either water or anions in solution.
Journal ArticleDOI
Electron transfer with no dissociation ion mobility–mass spectrometry (ETnoD IM-MS). The effect of charge reduction on protein conformation
Jacquelyn R. Jhingree,Rebecca Beveridge,Eleanor R. Dickinson,Jonathan P. Williams,Jeffery Mark Brown,Bruno Bellina,Perdita E. Barran +6 more
TL;DR: In this article, a novel mass spectrometry approach is reported which investigates how ion-molecule charge reduction reactions between radical anions and protein cations modulate protein conformation.
Journal ArticleDOI
Combination of noncovalent mass spectrometry and traveling wave ion mobility spectrometry reveals sugar-induced conformational changes of central glycolytic genes repressor/DNA complex.
Cédric Atmanene,Denix Chaix,Yannick Bessin,Nathalie Declerck,Alain Van Dorsselaer,Sarah Sanglier-Cianférani +5 more
TL;DR: It is revealed that tetrameric CggR dissociates into dimers upon FBP binding and triggers disruption of intermolecular protein/protein interactions within the complex, significantly modifying its conformation as evidenced by a 5% increase of its collision cross section.
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