Application of electrospray ionization mass spectrometry for studying human immunodeficiency virus protein complexes.
Proteins
; Suppl 2: 28-37, 1998.
Article
de En
| MEDLINE
| ID: mdl-9849908
ABSTRACT
Mass spectrometry (MS) with electrospray ionization (ESI) has shown utility for studying noncovalent protein complexes, as it offers advantages in sensitivity, speed, and mass accuracy. The stoichiometry of the binding partners can be easily deduced from the molecular weight measurement. In many examples of protein complexes, the gas phase-based measurement is consistent with the expected solution phase binding characteristics. This quality suggests the utility of ESI-MS for investigating solution phase molecular interactions. Complexes composed of proteins from the human immunodeficiency virus (HIV) have been studied using ESI-MS. Multiply charged protein dimers from HIV integrase catalytic core (F185K) and HIV protease have been observed. Furthermore, the ternary complex between HIV protease dimer and inhibitor pepstatin A was studied as a function of solution pH. Zinc binding to zinc finger-containing nucleocapsid protein (NCp7) and the NCp7-psi RNA 11 stoichiometry complex was also studied by ESI-MS. No protein-RNA complex was observed in the absence of zinc, consistent with the role of the zinc finger motifs for RNA binding.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Protéines virales
/
Produits du gène gag
/
Capside
/
Protéase du VIH
/
Doigts de zinc
/
Intégrase du VIH
/
Protéines de capside
Limites:
Humans
Langue:
En
Journal:
Proteins
Sujet du journal:
BIOQUIMICA
Année:
1998
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique