Increasing charge while preserving noncovalent protein complexes for ESI-MS.
J Am Soc Mass Spectrom
; 20(4): 593-6, 2009 Apr.
Article
en En
| MEDLINE
| ID: mdl-19101165
ABSTRACT
Increased multiple charging of native proteins and noncovalent protein complexes is observed in electrospray ionization (ESI) mass spectra obtained from nondenaturing protein solutions containing up to 1% (vol/vol) m-nitrobenzyl alcohol (m-NBA). The increases in charge ranged from 8% for the 690 kDa alpha(7)beta(7)beta(7)alpha(7) 20S proteasome complex to 48% additional charge for the zinc-bound 29 kDa carbonic anhydrase-II protein. No dissociation of the noncovalently bound ligands/subunits was observed upon the addition of m-NBA. It is not clear if the enhanced charging is related to altered surface tension as proposed in the "supercharging" model of Iavarone and Williams (Iavarone, A. T.; Williams, E. R. J. Am. Chem. Soc.2003, 125, 2319-2327). However, more highly charged noncovalent protein complexes have utility in relaxing slightly the mass-to-charge (m/z) requirements of the mass spectrometer for detection and will be effective for enhancing the efficiency for tandem mass spectrometry studies of protein complexes.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas
/
Espectrometría de Masa por Ionización de Electrospray
Límite:
Animals
Idioma:
En
Revista:
J Am Soc Mass Spectrom
Año:
2009
Tipo del documento:
Article
País de afiliación:
Estados Unidos