Probing protein stabilization by glycerol using electrospray mass spectrometry.
J Mass Spectrom
; 36(8): 918-22, 2001 Aug.
Article
en En
| MEDLINE
| ID: mdl-11523091
This study shows that electrospray ionization mass spectrometry (ESI-MS), combined with a heated turbo ion-spray interface, allows monitoring protein stabilization by glycerol in solution. Measurements obtained with the two proteins lysozyme and cytochrome c are presented. The observed mass-to-charge (m/z) distributions reveal the stabilizing effect of the additive on the protein conformations against temperature and acid-induced unfolding, as well as against denaturation by acetonitrile. The data obtained with lysozyme allow detection of minor conformational changes upon glycerol addition to the native protein, and suggest that the protein structure in the presence of the additive is slightly compressed compared with its state in water. This result corroborates previous evidence obtained by nuclear magnetic resonance. It is also shown that analysis of the m/z distributions obtained by ESI-MS can lead to detection of partially folded and partially populated states in protein samples.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Bradiquinina
/
Proteínas
/
Muramidasa
/
Grupo Citocromo c
/
Glicerol
Límite:
Animals
Idioma:
En
Revista:
J Mass Spectrom
Año:
2001
Tipo del documento:
Article
País de afiliación:
Austria
Pais de publicación:
Reino Unido