STUDYING NONCOVALENT PROTEIN COMPLEXES BY ELECTROSPRAY-IONIZATION MASS-SPECTROMETRY

Authors
Citation
Ja. Loo, STUDYING NONCOVALENT PROTEIN COMPLEXES BY ELECTROSPRAY-IONIZATION MASS-SPECTROMETRY, Mass spectrometry reviews, 16(1), 1997, pp. 1-23
Citations number
183
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Spectroscopy
Journal title
ISSN journal
0277-7037
Volume
16
Issue
1
Year of publication
1997
Pages
1 - 23
Database
ISI
SICI code
0277-7037(1997)16:1<1:SNPCBE>2.0.ZU;2-A
Abstract
Electrospray ionization mass spectrometry has been used to study prote in interactions driven by noncovalent forces. The gentleness of the el ectrospray ionization process allows intact protein complexes to be di rectly detected by mass spectrometry. Evidence from the growing body o f literature suggests that the ESI-MS observations for these weakly bo und systems reflect, to some extent, the nature of the interaction fou nd in the condensed phase. Stoichiometry of the complex can be easily obtained from the resulting mass spectrum because the molecular weight of the complex is directly measured. Far the study of protein interac tions, ESI-MS is complementary to other biophysical methods, such as N MR and analytical ultracentrifugation. However, mass spectrometry offe rs advantages in speed and sensitivity. The experimental variables tha t play a role in the outcome of ESI-MS studies of noncovalently bound complexes are reviewed. Several applications of ESI-MS are discussed, including protein interactions with metal ions and nucleic acids and s ubunit protein structures (quaternary structure). (C) 1997 John Wiley Sons, Inc.