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Barry K. Carpenter

Researcher at Cardiff University

Publications -  183
Citations -  8200

Barry K. Carpenter is an academic researcher from Cardiff University. The author has contributed to research in topics: Potential energy surface & Dissociation (chemistry). The author has an hindex of 46, co-authored 181 publications receiving 7742 citations. Previous affiliations of Barry K. Carpenter include Academy of Sciences of the Czech Republic & Astra.

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Electron Capture Dissociation for Structural Characterization of Multiply Charged Protein Cations

TL;DR: 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.
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Electron Capture Dissociation of Gaseous Multiply-Charged Proteins Is Favored at Disulfide Bonds and Other Sites of High Hydrogen Atom Affinity

TL;DR: RRKM calculations indicate that H• capture Dissociation of backbone bonds in multiply-charged proteins represents nonergodic behavior, as proposed for the original direct mechanism of electron capture dissociation.
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Electron capture dissociation of gaseous multiply charged ions by Fourier-transform ion cyclotron resonance.

TL;DR: 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.
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Identification and quantification of kynurenic acid in human brain tissue.

TL;DR: Serial ion-exchange and high-performance liquid chromatography separations were employed for the tissue extraction and purification of kynurenic acid (KYNA) and the compound isolated from postmortem human brain tissue was unequivocally identified as KYNA by nuclear magnetic resonance and mass spectrometric analyses.
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Secondary and tertiary structures of gaseous protein ions characterized by electron capture dissociation mass spectrometry and photofragment spectroscopy.

TL;DR: Photofragmentation of ECD-reduced ubiquitin ions shows that only the 6+ to 9+, not the 10+ to 13+ ions, have tertiary noncovalent bonding; this is indicated as hydrogen bonding by the 3,050–3,775 cm−1 photofragment spectrum.