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Titolo:
Activated ion electron capture dissociation for mass spectral sequencing of larger (42 kDa) proteins
Autore:
Horn, DM; Ge, Y; McLafferty, FW;
Indirizzi:
Cornell Univ, 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: 20, volume: 72, anno: 2000,
pagine: 4778 - 4784
SICI:
0003-2700(20001015)72:20<4778:AIECDF>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
INFRARED MULTIPHOTON DISSOCIATION; MULTIPLY-CHARGED IONS; POSTTRANSLATIONAL MODIFICATIONS; RADIATIVE DISSOCIATION; IDENTIFYING PROTEINS; THIAMINASE-I; SPECTROMETRY; IDENTIFICATION; IONIZATION; BIOMOLECULES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: McLafferty, FW Cornell Univ, Dept Chem & Biol Chem, Ithaca, NY 14853 USA Cornell Univ Ithaca NY USA 14853 hem, Ithaca, NY 14853 USA
Citazione:
D.M. Horn et al., "Activated ion electron capture dissociation for mass spectral sequencing of larger (42 kDa) proteins", ANALYT CHEM, 72(20), 2000, pp. 4778-4784

Abstract

In previous studies, electron capture dissociation (ECD) has been successful only with ionized smaller proteins, cleaving between 33 of the 153 aminoacid pairs of a 17 kDa protein. This has been increased to 99 cleavages bycolliding the ions with a background gas while subjecting them to electroncapture. Presumably this ion activation breaks intramolecular noncovalent bonds of the ion's secondary and tertiary structure that otherwise prevent separation of the products from the nonergodic ECD cleavage of a backbone covalent bond. In comparison to collisionally activated dissociation, this "activated ion" (AI) ECD provides more extensive, and complementary, sequence information. AI ECD effected cleavage of 116, 60, and 47, respectively, backbone bonds in 29, 30, and 42 kDa proteins to provide extensive contiguous sequence information on both termini; AI conditions are being sought to denature the center portion of these large ions, This accurate "sequence tag" information could potentially identify individual proteins in mixtures atfar lower sample levels than methods requiring prior proteolysis.

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Documento generato il 26/09/20 alle ore 14:49:46