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Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process
Neutralization-reionization mass spectrometry (MS)1 is of unique value for preparing and characterizing highly reactive and unstable neutral species, such as the intermediate in theExpand
Electron capture dissociation for structural characterization of multiply charged protein cations.
For proteins of < 20 kDa, this new radical site dissociation method cleaves different and many more backbone bonds than the conventional MS/MS methods that add energy directly to the even-electron ions. Expand
Electron Capture Dissociation of Gaseous Multiply-Charged Proteins Is Favored at Disulfide Bonds and Other Sites of High Hydrogen Atom Affinity
Disulfide bonds in gaseous multiply-protonated proteins are preferentially cleaved in the mass spectrometer by low-energy electrons, in sharp contrast to excitation of the ions by photons orExpand
Reactions of polypeptide ions with electrons in the gas phase.
  • R. Zubarev
  • Chemistry, Medicine
  • Mass spectrometry reviews
  • 2003
Reactions of electrons in the energy range below 70 eV with polypeptide cations and anions are reviewed, as well as their applications for the structural analysis of polypeptides. At very lowExpand
Electron-capture dissociation tandem mass spectrometry.
  • R. Zubarev
  • Chemistry, Medicine
  • Current opinion in biotechnology
  • 1 February 2004
In biotechnology, the main area of ECD application is expected to be the top-down verification of DNA-predicted protein sequences, de novo sequencing, disulfide bond analysis and the combined bottom-up analysis of post-translational modifications. Expand
Electron detachment dissociation of peptide di-anions: an electron–hole recombination phenomenon
A novel electron–ion reaction mimicking positron capture is reported for gas-phase polypeptide di-anions. Bombardment of the latter by >10 eV electrons produced electron detachment followed byExpand
Orbitrap mass spectrometry.
Orbitrap is the newest addition to the family of high-resolution mass spectrometry analyzers, combining high speed with excellent quantification properties, ranking favorably in many analytical applications. Expand
The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERAD.
It is shown that RFP2 contains a C-terminal transmembrane domain indispensable for its localization to the ER and that Rfp2 colocalizes with several ER-resident proteins as analyzed by high-resolution immunostaining, consistent with a function for R FP2 as an ERAD E3 ubiquitin ligase. Expand
Localization of labile posttranslational modifications by electron capture dissociation: the case of gamma-carboxyglutamic acid.
ECD is a unique complement to conventional methods for MS/MS, causing less undesirable loss of side-chain functionalities as well as more desirable backbone cleavages. Expand
Electron capture dissociation of gaseous multiply charged ions by Fourier-transform ion cyclotron resonance
High specificity for covalent bond cleavage makes ECD promising for studying the secondary and tertiary structure of gaseous protein ions caused by noncovalent bonding, and highly complementary to the well known energetic methods for multiply charged ion dissociation. Expand