Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Gas-phase binding of non-covalent protein complexes between bovine pancreatic trypsin inhibitor and its target enzymes studied by electrospray ionization tandem mass spectrometry
Autore:
Nesatyy, VJ;
Indirizzi:
Univ British Columbia, Dept Chem, Vancouver, BC V6T 1Z1, Canada Univ British Columbia Vancouver BC Canada V6T 1Z1 ver, BC V6T 1Z1, Canada
Titolo Testata:
JOURNAL OF MASS SPECTROMETRY
fascicolo: 8, volume: 36, anno: 2001,
pagine: 950 - 959
SICI:
1076-5174(200108)36:8<950:GBONPC>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLLISION CROSS-SECTIONS; NONCOVALENT COMPLEXES; CRYSTAL-STRUCTURES; RECOGNITION SITES; LIGAND-BINDING; CHYMOTRYPSIN; IONS; DISSOCIATION; SPECIFICITY; ANTIBIOTICS;
Keywords:
protein; non-covalent complexes; electrospray ionization; collisionally activated dissociation; tandem mass spectrometry;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Nesatyy, VJ Natl Res Council Canada, Inst Marine Biosci, 1411 Oxford St, Halifax, NS B3H 3Z1, Canada Natl Res Council Canada 1411 Oxford St Halifax NS Canada B3H 3Z1
Citazione:
V.J. Nesatyy, "Gas-phase binding of non-covalent protein complexes between bovine pancreatic trypsin inhibitor and its target enzymes studied by electrospray ionization tandem mass spectrometry", J MASS SPEC, 36(8), 2001, pp. 950-959

Abstract

The potential of electrospray ionization (ESI) mass spectrometry (MS) to detect non-covalent protein complexes has been demonstrated repeteadly. However, questions about correlation of the solution and gas-phase structures of these complexes still produce vigorous scientific discussion. Here, we demonstrate the evaluation of the gas-phase binding of non-covalent protein complexes formed between bovine pancreatic trypsin inhibitor (BPTI) and its target enzymes over a wide range of dissociation constants. Non-covalent protein complexes were detected by ESI-MS. The abundance of the complex ions in the mass spectra is less than expected from the values of the dissociation constants of the complexes in solution. Collisionally activated dissociation (CAD) tandem mass spectrometry (MS/MS) and a collision model for ion activation were used to evaluate the binding of non-covalent complexes in the gas phase. The internal energy required to induce dissociation was calculated for three collision gases (Ne, Ar, Kr) over a wide range of collision gas pressures and energies using an electrospray ionization source. The order of binding energies of the gas-phase ions for non-covalent protein complexes formed by the ESI source and assessed using CAD-MS/MS appears to differ from that of the solution complexes. The implication is that solution structure of these complexes was not preserved in the gas phase. Copyright (C)2001 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 13:59:53