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Titolo:
Electron capture dissociation for structural characterization of multiply charged protein cations
Autore:
Zubarev, RA; Horn, DM; Fridriksson, EK; Kelleher, NL; Kruger, NA; Lewis, MA; Carpenter, BK; McLafferty, FW;
Indirizzi:
Cornell Univ, Baker Lab, Dept Chem & Biol Chem, Ithaca, NY 14853 USA Cornell Univ Ithaca NY USA 14853 t Chem & Biol Chem, Ithaca, NY 14853 USA
Titolo Testata:
ANALYTICAL CHEMISTRY
fascicolo: 3, volume: 72, anno: 2000,
pagine: 563 - 573
SICI:
0003-2700(20000201)72:3<563:ECDFSC>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
TANDEM MASS-SPECTROMETRY; CYTOCHROME-C IONS; LARGE MOLECULES; IDENTIFICATION; BIOMOLECULES; EXCITATION; CHEMISTRY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: McLafferty, FW Cornell Univ, Baker Lab, Dept Chem & Biol Chem, Ithaca, NY 14853 USA Cornell Univ Ithaca NY USA 14853 hem, Ithaca, NY 14853 USA
Citazione:
R.A. Zubarev et al., "Electron capture dissociation for structural characterization of multiply charged protein cations", ANALYT CHEM, 72(3), 2000, pp. 563-573

Abstract

For proteins of < 20 kDa, this new radical site dissociation method-cleaves different and many more backbone bonds than the conventional MS/MS methods (e.g, collisionally activated dissociation, CAD) that add energy directlyto the even-electron ions. A minimum kinetic energy difference between theelectron and ion maximizes capture; a 1 eV difference reduces capture by 10(3). Thus, in an FTMS ion cell with added electron trapping electrodes, capture appears to be achieved best at the boundary between the potential wells that trap the electrons and ions, now providing 80 +/- 15% precursor ionconversion efficiency. Capture cross section is dependent on the ionic charge squared (z(2)), minimizing the secondary dissociation of lower charge fragment ions. Electron capture is postulated to occur initially at a protonated site to release an energetic (similar to 6 eV) H-. atom that is captured ata high-affinity site such as -S-S- or backbone amide to cause nonergodic (before energy randomization) dissociation. Cleavages between every pairof amino acids in mellitin (2.8 kDa) and ubiquitin (8.6 kDa) are represented in their ECD and CAD spectra, providing complete data for their de novo sequencing. Because posttranslational modifications-such as carboxylation, glycosylation, and sulfation are less easily lost in ECD than in CAD, ECD assignments of their sequence positions are far more specific.

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Documento generato il 05/07/20 alle ore 09:18:52