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Titolo:
Proton affinities of the commonly occuring L-amino acids by using electrospray ionization-ion trap mass spectrometry
Autore:
Afonso, C; Modeste, F; Breton, P; Fournier, F; Tabet, JC;
Indirizzi:
Univ Paris 06, UMR 7613, F-75252 Paris 05, France Univ Paris 06 Paris France 05 ris 06, UMR 7613, F-75252 Paris 05, France Ctr Etud Bouchet, F-91710 Vert Le Petit, France Ctr Etud Bouchet Vert Le Petit France F-91710 1710 Vert Le Petit, France
Titolo Testata:
EUROPEAN JOURNAL OF MASS SPECTROMETRY
fascicolo: 5, volume: 6, anno: 2000,
pagine: 443 - 449
SICI:
1469-0667(2000)6:5<443:PAOTCO>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
GAS-PHASE BASICITIES; KINETIC METHOD; THERMOCHEMICAL DETERMINATIONS; FOURIER-TRANSFORM; BOUND DIMERS; PEPTIDES; DISSOCIATION; TEMPERATURE; HISTIDINE; LYSINE;
Keywords:
kinetic method; ion trap; effective temperature; amino acids; proton affinity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Tabet, JC Univ Paris 06, UMR 7613, 2-LCSOB,Bat F,Boite 45,4 Pl Jussieu, F-75252 Paris 05, France Univ Paris 06 2-LCSOB,Bat F,Boite 45,4 Pl Jussieu Paris France 05
Citazione:
C. Afonso et al., "Proton affinities of the commonly occuring L-amino acids by using electrospray ionization-ion trap mass spectrometry", EUR J MASS, 6(5), 2000, pp. 443-449

Abstract

In this study, the use of an electrospray ionization (ESI)-ion trap mass spectrometry to perform thermochemical determinations using the kinetic method is shown. In this method, competitive dissociations of selected proton-bound heterodimeric [BiHB](+) ions are investigated and particularly, the product ion abundance [BiH+] / [BH+] ratio is accurately measured and compared to the proton affinity of each neutral partner (i.e. the B-i and B), The proton affinities of the amino acids are well known and these compounds were chosen to investigate the ion trap potentiality for such purpose, particularly, when externally prepared ions were injected. It appears that, in spite of the low abundance of home and heterodimer ions, constant and reproducible [BiH+] / [BH+] ratios are obtained when sequential tandem mass spectrometry (MS/MS) experiments are performed within similar ion trapping conditions. Such conditions are reached for a constant ion excitation q(z) value. The resulting ln([BiH+] / [BH+]) dependence upon the PA(Bi) and PA(B) values (from the literature) is linear and yields a reproducible slope after several measurements are made to determine the accuracy of this approach. Under various excitation conditions, in spite of the change in effective temperature, neither the scale order nor the PA values are changed. Furthermore, entropy variation (S-0) between leucine and other amino acids was evaluatedby several methods.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 09:34:31